АТФазный домен в транспортных белках вирусов растений тема диссертации и автореферата по ВАК РФ 03.00.06, кандидат биологических наук Лещинер, Анна Дмитриевна
- Специальность ВАК РФ03.00.06
- Количество страниц 134
Оглавление диссертации кандидат биологических наук Лещинер, Анна Дмитриевна
Список сокращений.
Введение.
Обзор литературы:.
Многокомпонентные транспортные системы вирусов растений.
Транспорт вирусов с тройным блоком транспортных генов.
Особенности транспортной системы гордеи-подобных вирусов.
Особенности транспортной системы потекс-подобных вирусов.
Потивирусы.
Клостеровирусы.
Материалы и методы.
Результаты.
Обсуждение.
Выводы.
Рекомендованный список диссертаций по специальности «Вирусология», 03.00.06 шифр ВАК
Функции цистеин-богатых белков гордеивирусов2003 год, кандидат биологических наук Елина, Наталия Эдгардовна
Экспрессия консервативных антигенов вируса гриппа A в растениях на поверхности химерных частиц ВТМ: иммуногенные и протективные свойства кандидатных вакцин2013 год, кандидат биологических наук Петухова, Наталья Витальевна
Исследование роли транспорта макромолекул в бактериальном и вирусном патогенезе растений и создание биотехнологической платформы продукции фармацевтических белков2013 год, доктор биологических наук Комарова, Татьяна Валерьевна
Участок внутренней посадки рибосом гена белка оболочки вируса табачной мозаики крестоцветных2006 год, кандидат биологических наук Комарова, Татьяна Валерьевна
Сборка трастузумаб (герцептин)-связывающих наночастиц вируса табачной мозаики в листьях: Nicotiana benthamiana2010 год, кандидат биологических наук Петруня, Игорь Валерьевич
Заключение диссертации по теме «Вирусология», Лещинер, Анна Дмитриевна
Выводы
1. В составе НТФазно/хеликазных доменов ТБГ1 транспортных белков двух групп вирусов с тройным блоком транспортных генов - потексвируса X-вируса картофеля и гордеивируса полулатентного вируса мятлика выявлен минимальный субдомен, отвечающий за АТФазную активность белков.
2. Выявленный субдомен способен неспецифически и кооперативно взаимодействовать с РНК и образовывать гомоолигомеры.
3. Мутация консервативного остатка основной аминокислоты перед мотивом I не влияет на АТФазную активность минимального субдомена, но понижает эту активность полноразмерного НТФазно/хеликазного домена у вирусов обеих групп.
4. Рекомбинантный белок оболочки потивируса А-вируса картофеля, участвующего в транспорте вирусного генома, обладает Mg^-зависимой НТФазной активностью in vitro. Участок, отвечающий за данную активность, скорее всего, локализуется в С-концевой половине белка.
Благодарности
Искренне благодарю мою научную руковолительницу Наталию Олеговну Калинину, заведующего лабораторией Сергея Юрьевича Морозова, а также Андрея Геннадьевича Соловьева. Особая благодарность заведующему кафедрой вирусологии и отдела биохимии вирусов растений за предоставление возможности проведения данной работы. Благодарю всех сотрудников кафедры вирусологии за неоценимую помощь и поддержку во время выполнения данной работы. Отдельная благодарность Марине Владимировне Архипенко, Евгению Николаевичу Доброву, Роману Алексеевичу Зиновкину, Петру Алексеевичу Иванову, Татьяне Валерьевне Комаровой, Нине Иосифовне Луховицкой, Елене Алексеевне Мининой, Виктору Александровичу Новикову, Дарье Викторовне Ракитиной, Евгению Владимировичу Скурату, Татьяне Юрьевне Тилькуновой, Михаилу Вячеславовичу Щепетильникову.
Список литературы диссертационного исследования кандидат биологических наук Лещинер, Анна Дмитриевна, 2006 год
1. Alzhanova D.V, Napuli A.J, Creamer R. and Dolja V.V. (2001). Cell-to-cell movement and assembly of a plant closterovirus: roles for the capsid proteins and Hsp70 homolog. EMBO J, 20, 6997-7007.
2. Andrejeva J, Jarvekulg L, Rabenstein F, Torrance L, Harrison B.D, Saarma M. (1994). Antigenic analysis of potato virus A particles and coat protein. Ann Appl Biol, 125, 337-348.
3. Angell S.M, Davies C. and Baulcombe D.C. (1996). Cell-to-cell movement of potato virus X is associated with a change in the size-exclusion limit of plasmodesmata in trichome cells of Nicotiana clevelandii. Virology, 216, 197-201.
4. Atabekov J.G. and Dorokhov Yu.L. (1984). Plant virus-specific transport function and resistance of plants to viruses. Adv Virus Res, 29, 313364.
5. Atabekov J.G. and Taliansky M.E. (1990). Expression of a plant virus-coded transport function by different viral genomes. Adv Virus Res, 38, 201-248.
6. Atabekov J.G, Rodionova N.P, Karpova O.V, Kozlovsky S.V. and Poljakov V.Y. (2000). The movement protein-triggered in situ conversion of potato virus X virion RNA from a nontranslatable into a translatable form. Virology, 271, 259-263.
7. Atabekov J.G, Rodionova N.P, Karpova O.V, Kozlovsky S.V, Novikov V.K, Arkhipenko M.V. (2001). Translational activation of encapsidated potato virus X RNA by coat protein phosphorylation. Virology, 286(2), 466-474.
8. Baratova L.A, Efimov A.V, Dobrov E.N, Fedorova N.V, Hunt R, Badun G.A, Ksenofontov A.L, Torrance L, Jarvekulg L. (2001). In Situ spatial organization of potato virus A coat protein subunits as assessed by tritium bombardment. J Virol, 75, 9696-9702.
9. Baulcombe D. (2002). Viral suppression of systemic silencing. Trends in Microbiology, 10, 306-308.
10. Baulcombe D.C., Chapman S. and Santa Cruz S. (1995). Jellyfish green fluorescent protein as a reporter for virus infections. Plant J, 7, 10451053.
11. Bayne E.H., Rakitina D.V., Morozov S. Yu., Baulcombe D.C. (2005). Cell-to-cell movement of potato potexvirus X is dependent on suppression of RNA silencing. Plant J, 44(3), 471-82.
12. Beck. D.L., Guilford P.J., Voot D.M., Andersen M.T. and Forster R.L. (1991). Triple gene block proteins of white clover mosaic potexvirus are required for transport. Virology, 183, 695-702.
13. Blackman L.M. and Overall R.L. (2001). Structure and function of plasmodesmata. Australian Journal of Plant Physiology, 28, 709-727.
14. Bleykasten C., Gilmer D., Guilley H., Richards K.E. and Jonard G. (1996). Beet necrotic yellow vein virus 42 kDa triple gene block protein binds nucleic acid in vitro. J Gen Virol, 77(5), 889-897.
15. Boyko V., Ferralli J., Ashby J., Schellenbaum P., Heinlein M. (2000b). Function of microtubules in intercellular transport of plant virus RNA. Nat Cell Biol, 2(11), 826-32.
16. Boyko V., van der Laak J., Ferralli J., Suslova E., Kwon M.O., Heinlein M. (2000a). Cellular targets of functional and dysfunctional mutants of tobacco mosaic vims movement protein fused to green fluorescent protein. J Virol, 74(23), 11339-46.
17. Brakke M.K., Ball E.M. and Langenberg W.G. (1988). A non-capsid protein associated with unencapsidated virus RNA in barley infected with barley stripe mosaic virus. J Gen Virol, 69,481-491.
18. Callaway A., Giesman-Cookmeyer D., Gillock E.T., Sit T.L. and Lommel S.A. (2001). The multifunctional capsid proteins of plant viruses. Annu Rev Phytopathol, 39, 419-460.
19. Carrington J.C, Jensen P.E. and Schaad M.C. (1998). Genetic evidence for an essential role for potyvirus CI protein in cell-to-cell movement. Plant J, 14, 393-400.
20. Carrington J.C., Kasschau K.D. and Johansen L.K. (2001). Activation and suppression of RNA silencing by plant viruses. Virology, 281, 1-5.
21. Carrington J.C., Kasschau K.D., Mahajan S.K., and Schaad M.C. (1996). Cell-to-cell and long-distance transport of viruses in plants. Plant Cell, 8, 1669-1681.
22. Caruthers J.M. and McKay D. (2002). Helicase structure and mechanism. Curr Opin Struct Biol, 12, 123-133.
23. Caruthers J.M., Johnson E.R., McKay D.B. (2000). Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc Natl Acad Sci USA, 97(24), 13080-5.
24. Chapman S., Hills G, Watts J. and Baulcombe D. (1992). Mutational analysis of the coat protein gene of potato virus X, effects on virion morphology and viral pathogenicity. Virology, 191, 223-230.
25. Cho H.S., Ha N.C., Kang L.W., Chung K.M., Back S.H., Jang S.K., Oh B.H. (1998). Crystal structure of RNA helicase from genotype lb hepatitis C virus. A feasible mechanism of unwinding duplex RNA. J Biol Chem, 273(24), 15045-52.
26. Citovsky V. and Zambryski P. (1991). How do plant virus nucleic acids move through intercellular connections? Bioessays, 13(8), 373-379.
27. Citovsky V., Knorr D., Schuster G. and Zambryski P. (1990). The P30 movement protein of tobacco mosaic virus is a single-strand nucleic acid binding protein. Cell, 60(4), 637-647.
28. Cowan G.H, Lioliopoulou R., Ziegler A., Torrance L. (2002). Subcellular localisation, protein interactions, and RNA binding of Potato mop-top virus triple gene block proteins. Virology, 298(1), 106-15.
29. Cronin S., Verchot J., Haldeman-Cahill R., Schaad M.C., Carrington J.C. (1995). Long-distance movement factor: a transport function of the potyvirus helper component proteinase. Plant Cell, 7(5), 549-59.
30. Daneholt B. (2001). Assembly and transport of a premessenger RNP particle. Proc Natl Acad Sci USA, 98(13), 7012-7017.
31. Daros J.A. and Carrington J.C. (1997). RNA binding activity of Nia proteinase of tobacco etch potyvirus. Virology, 237(2), 327-36.
32. Dawson W.O., Bubrick P., Grantham G.L. (1988). Modification of the tobacco mosaic virus coat protein gene affecting replication movement and symptomatology. Phytopatol, 78, 783-789.
33. Deom C.M., Lapidot M., Beachy R.N. (1992). Plant virus movement protein. Cell, 69, 221-224.
34. Ding B, Li Q, Nguyen L, Palukaitis P. and Lucas W.J. (1995). Cucumber mosaic virus 3 a protein potentiates cell-to-cell trafficking of CMV RNA in tobacco plants. Virology, 207, 345-353.
35. Dolja V.V, Boyko V.P., Agranovsky A.A, Koonin E.V. (1991). Phylogeny of capsid proteins of rod-shaped and filamentous RNA plant viruses: two families with distinct patterns of sequence and probably structure conservation. Virology, 184(1), 79-86.
36. Dolja V.V, Haldeman R, Robertson N.L, Dougherty W.G, Carrington J.C. (1994). Distinct functions of capsid protein in assembly and movement of tobacco etch potyvirus in plants. EMBOJ, 13, 1482-1491.
37. Dolja V.V, Haldeman-Cahill R, Montgomery A.E, Vandenbosch K.A, Carrington J.C. (1995). Capsid protein determinants involved in cell-to-cell and long distance movement of tobacco etch potyvirus. Virology, 206, 1007-1016.
38. Dolja V.V, Kreuze J.F, Valkonen J.P.T. (2006). Comparative and functional genomics of closteroviruses. Virus Res, 117, 38-51.
39. Donald R.G, Lawrence D.M. and Jackson A.O. (1997). The barley stripe mosaic virus 58-kilodalton beta(b) protein is a multifunctional RNA binding protein. J Virol, 71(2), 1538-1546.
40. Donald R.G, Zhou H, Jackson A.O. (1993). Serological analysis of barley stripe mosaic virus-encoded proteins in infected barley. Virology, 195(2), 659-68.
41. Dunoyer P, Thomas C, Harrison S, Revers F, Maule A. (2004). A cysteine-rich plant protein potentiates Potyvirus movement through an interaction with the virus genome-linked protein VPg. J Virol, 78(5), 2301-9.
42. Efimov A.V. (1991). Structure of coiled beta-beta-hairpins and betabeta-corners. FEBS Lett, 284(2), 288-92.
43. Erhardt M, Stussi-Garaud C, Guilley H, Richards K.E, Jonard G. and Bouzoubaa S. (1999). The first triple gene block protein of peanut clump virus localizes to the plasmodesmata during virus infection. Virology, 264(1), 220-229.
44. Fedorkin O.N, Solovyev A.G, Yelina N.E, Zamyatnin A.A, Zinovkin R.A, Makinen K, Schiemann J, Morozov S.Yu. (2001). Cell-to-cell movement of potato virus X involves distinct functions of the coat protein. J Gen Virol, 82,449-458.
45. Fedoroff N. (2002). RNA-binding proteins in plants: the tip of an iceberg? Curr Opin Plant Biol, 5, 452-459.
46. Fernandez A, Guo H.S, Saenz P, Simon-Buela L, Gomez de Cedrón M, Garcia J. A. (1997). The motif V of plum pox potyvirus CI RNA helicase is involved in NTP hydrolysis and is essential for virus RNA replication. Nucleic Acids Res, 25(22), 4474-80.
47. Forster R.L, Beck D.L, Guilford P.I, Voot D.M, Van Dolleweerd C.J. and Andersen M.T. (1992). The coat protein of white clover mosaic potexvirus has a role in facilitating cell-to-cell transport in plants. Virology, 191(1), 480-484.
48. Fridborg I, Grainger J, Page A, Coleman M, Findlay K. and Angelí S. (2003). TIP, a novel host factor linking callóse degradation with the cell-to-cell movement of Potato virus X. Mol Plant Microbe Interact, 16, 132140.
49. Gao Z, Johansen E, Eyers S, Thomas C.L, Noel Ellis T.H, Maule A.J. (2004). The potyvirus recessive resistance gene, sbml, identifies a novel role for translation initiation factor eIF4E in cell-to-cell trafficking. Plant J, 40(3), 376-85.
50. Ghoshroy S., Lartey R., Sheng J. and Citovsky V. (1997). Transport of proteins and nucleic acids through plasmodesmata. Ann Rev in Plant Physiol and Plant Mol Biol, 48, 27-49.
51. Gilmer D., Bouzoubaa S., Hehn A., Guilley H., Richards K. and Jonard G. (1992a). Efficient cell-to-cell movement of beet necrotic yellow vein virus requires 3'- proximal genes located on RNA 2. Virology, 189, 4047.
52. Gorbalenya A.E. and Koonin E.V. (1993). Helicases, amino acid sequence comparisons and structure-function relationships. Curr Opin Cell Biol, 3, 419-429.
53. Gorbalenya A.E., Blinov V.M, Donchenko A.P. and Koonin E.V. (1989). An NTP-binding motif is the most conserved sequence in a highly diverged nionophyletic group of proteins involved in positive strand RNA viral replication. J Mol Evol, 28(3), 256-268.
54. Goregaoker S.P., Culver J.N. (2003). Oligomerization and activity of the helicase domain of the tobacco mosaic virus 126- and 183-kilodalton replicase proteins. J Virol, 77(6), 3549-56
55. Graves-Woodward K.L., Weller S.K. (1996). Replacement of gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicase-primase. J Biol Chem, 271(23), 13629-35.
56. Hall M.C., Matson S.W. (1999) Helicase motifs, the engine that powers DNA unwinding. Mol Microbiol, 34(5), 867-77.
57. Hamilton W.D.O. and Baulcombe D.C. (1989). Infectious RNA produced by in vitro transcription of a full-length tobacco rattle virus RNA-1 cDNA. J Gen Virol, 70, 963-968.
58. Haupt S., Cowan G.H., Ziegler A., Roberts A.G., Oparka K.J., Torrance L. (2005). Two plant-viral movement proteins traffic in the endocytic recycling pathway. Plant Cell, 17(1), 164-81.
59. Haywood V, Kragler F. and Lucas W.J. (2002). Plasmodesmata: Pathways for Protein and Ribonucleoprotein Signaling. Plant Cell, Suppl, 303-325.
60. Hefferon K.L, Doyle S. and AbouHaidar M.G. (1997). Immunological detection of the 8K protein of potato virus X (PVX) in cell walls of PYX-infected tobacco and transgenic potato. Arch Virol, 142, 425433.
61. Heinlein M. (2002a). The spread of tobacco mosaic virus infection: insights into the cellular mechanism of RNA transport. Cell Mol Life Sci, 59, 58-82.
62. Heinlein M. (2002b). Plasmodesmata: dynamic regulation and role in macromolecular cell-to-cell signaling. Curr Opin Plant Biol, 5, 1-10.
63. Herzog E, Hemmer O, Hauser S, Meyer G, Bouzoubaa S. and Fritsch C. (1998). Identification of genes involved in replication and movement of peanut clump virus. Virology, 248, 312-322.
64. Hull R. (1989). The movement of viruses in plant. Annua Rev Phytopathol, 27, 213-240.
65. Jankowsky E, Gros C.H, Shuman S. and Pyle A.M. (2001). Active disruption of an RNA-protein interaction by a DexH/D RNA helicase. Science, 291, 121-125.
66. Juuti J.T, Bamford D.H, Turna R. and Thomas G.J.Jr. (1998). Structure and NTPaseactivity of the RNA-translocatmg protein (P4) of bacteriophage phi 6. J Mol Biol, 279, 347-359.
67. Kadare G. and Haenni A-L. (1997). Virus-encoded RNA helicases. J Virol, 71, 2583-2590.
68. Kalinina N.O, Fedorkin O.N, Samuilova O.V, Maiss E, Korpela T, Morozov S.Yu. and Atabekov J.G. (1996). Expression and biochemical analyses of the recombinant potato virus X 25K movement protein. FEBS Lett, 397, 75-78.
69. Kalinina N.O, Rakitina D.V, Solovyev A.G, Schiemann J. and Morozov S.Yu. (2002). RNA helicase activity of the plant virus movement proteins encoded by the first gene of the triple gene block. Virology, 296, 321-329.
70. Kalinina N.O., Samuilova O.V., Fedorkin O.N., Zelenina D.A., Morozov S.Yu. (1998). Characteristics and subcellular localization of the 25 kDa protein of potato virus X. Mol biol, 4, 686-691.
71. Karasev A.V. (2000). GENETIC DIVERSITY AND EVOLUTION OF CLOSTEROVIRUSES. Annu Rev Phytopathol, 38, 293-324.
72. Karpova O.V., Rodionova N.P., Ivanov K.I., Kozlovsky S.V., Dorokhov Y.L., Atabekov J.G. (1999). Phosphorylation of tobacco mosaic virus movement protein abolishes its translation repressing ability. Virology, 261(1), 20-24.
73. Kasschau K.D., Cronin S., Carrington J.C. (1997). Genome amplification and long-distance movement functions associated with the central domain of tobacco etch potyvirus helper component-proteinase. Virology, 228, 251-262.
74. Kawakami S., Watanabe Y., Beachy R.N. (2004). Tobacco mosaic virus infection spreads cell to cell as intact replication complexes. Proc Natl AcadSci USA, 101(16): 6291-6.
75. Kim J.Y., Rim Y., Wang J., Jackson D. (2005). A novel cell-to-cell trafficking assay indicates that the KNOX homeodomain is necessary and sufficient for intercellular protein and mRNA trafficking. Genes Dev, 19(7), 788-93.
76. Kim J.Y., Yuan Z., Jackson D. (2003). Developmental regulation and significance of KNOX protein trafficking in Arabidopsis. Development, 130(18), 4351-62.
77. Kiselyova O.I., Yaminsky I.V., Karpova O.V., Rodionova N.P., Kozlovsky S.V., Arkhipenko M.V, Atabekov J.G. (2003). AFM study of potato virus X disassembly induced by movement protein. J Mol Biol, 332(2), 321-5.
78. Koenig R., Pleij C.W.,Loss S., Burgermeister W., Aust H., Schiemann J. (2004). Molecular characterisation of potexviruses isolated from three different genera in the family Cactaceae. Arch Virol, 149(5), 903-14.
79. Koenig R., Pleij C.W.A., Beier C. and Commandeur U. (1998). Genome properties of beet virus Q, a new furo-like virus from sugarbeet, determined from unpurified virus. J Gen Virol, 79, 2027-2036.
80. Koonin E.V. (2003). A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication. Nucleic Acids Res, 21(11), 2541-7.
81. Koonin E.V. and Dolja V.V. (1993). Evolution and taxonomy of positive-strand RNA viruses, implications of comparative analysis of amino acid sequences. Crit Rev Biochem Mol Biol, 28, 375-430.
82. Korolev S., Hsieh J, Gauss G.S, Lohman T.M., Waksman G. (1997). Major domain swiveling revealed by crystal structure of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell, 90, 635-647.
83. Kragler F., Monzer J., Shash K., Xoconostle-Cazares B. and Lucas W.J. (1998). Cell-to-cell transport of proteins: requirement for unfolding and characterization of binding to a putative plasmodesmal receptor. Plant J, 15, 367-381.
84. Krishnamurthy K., Heppler M., Mitra R., Blancaflor E., Payton M., Nelson R.S., Verchot-Lubicz J. (2003). The Potato virus X TGBp3 protein associates with the ER network for virus cell-to-cell movement. Virology, 309(1), 135-51.
85. Krishnamurthy K., Mitra R., Payton M.E. and Verchot-Lubicz J. (2002). Cell-to-cell movement of the PVX 12K, 8K, or coat proteins may depend on the host, leaf developmental stage, and the PVX 25K protein. Virology, 300,269-281.
86. Laemmli U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
87. Lawrence D.M and Jackson A.O. (2001). Interactions of the TGB1 protein during cell-to-cell movement of barley stripe mosaic virus. J Virol, 75(18), 8712-8723.
88. Lazarowitz S.G. and Beachy R.N. (1999). Viral movement proteins as probes for intracellular and intercellular trafficking in plants. Plant Cell, 11,535.548.
89. Leipe D.D, Wolf Y.I, Koonin E.V, Aravind L. (2002). Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol, 317(1), 41-72.
90. Leonard D.A. and Zaitlin M. (1982). A temperature-sensitive strain of tobacco mosaic virus defective in cell-to-cell movement generate an altered virus-coded protein. Virology, 117,416-424.
91. Lin M.K, Chang B.Y, Liao J.T, Lin N.S, Hsu Y.H. (2004). Arg-16 and Arg-21 in the N-terminal region of the triple-gene-block protein 1 of Bamboo mosaic virus are essential for virus movement. J Gen Virol, 85, 2519.
92. Lough T.J, Emerson S.J, Lucas W.J. and Forster R.L.S. (2001). Trans-complementation of long-distance movement of white clover mosaic virus triple gene block (TGB) mutants, phloem-associated movement of TGBpl. Virology, 288, 18-28.
93. Lucas W.J. (1995). Plasmodesmata: intercellular channels for macromolecular transport in plants. Curr Opin Cell Biol, 1, 673-680.
94. Lucas W.J. (1999). Plasmodesmata and the cell-to-cell transport of proteins and nucleoprotein complexes. J Exp Bot, 50, 979-987.
95. Lucas W.J. (2006). Plant viral movement proteins: agents for cell-to-cell trafficking of viral genomes. Virology, 344(1), 169-84.
96. Lucas W.J. and Lee J.Y. (2004). Plasmodesmata as a supracellular control network in plants. Nat Rev Mol Cell Biol, 5(9), 712-26.
97. Machius M., Henry L., Palnitkar M., Deisenhofer J. (1999). Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus. Proc Natl Acad Sci USA, 96(21), 11717-22.
98. Makino Y., Yamano K., Kanemaki M., Morikawa K., Kishimoto T., Shimbara N., Tanaka K., Tamura T. (1997). SUG1, a component of the 26 S proteasome, is an ATPase stimulated by specific RNAs. J Biol Chem, 272(37), 23201-5.
99. Malcuit I., Marano M.R., Kavanagh T.A., De Jong W., Forsyth A. and Baulcombe D.C. (1999). The 25-kDa movement protein of PVX elicits Nb-mediated hypersensitive cell death in potato. Mol Plant-Microbe Interact, 12, 536-543.
100. Mas P. and Beachy R.N. (1999). Replication of tobacco mosaic virus on endoplasmic reticulum and role of the cytoskeleton and virus movement protein in intracellular distribution of viral RNA .J Cell Biol, 147(5), 945-58.
101. McGeachy K.D., Barker H. (2000). Potato mop-top virus RNA can move long distance in the absence of coat protein: evidence from resistant, transgenic plants. Mol Plant-Microbe Interact, 13(1), 125-128.
102. Medina V, Peremyslov V.V., Hagiwara Y. and Dolja V.V. (1999). Subcellular localization of the HSP70-homolog encoded by beet yellows closterovirus. Virology, 260, 173-181.
103. Merai Z., Kerenyi Z., Kertesz S., Magna M., Lakatos L., Silhavy D. (2006). Double-stranded RNA binding may be a general plant RNA viral strategy to suppress RNA silencing. J Virol, 80(12), 5747-56.
104. Mitchell P. and Tollervey D. (2001). mRNA turnover. Curr Opin Cell Biol, 13, 320-325.
105. Morozov S.Y., Lukasheva L.I., Chernov B.K., Skryabin K.G. and Atabekov J.G. (1987). Nucleotide sequence of the open reading frames adjacent to the coat protein cistron in potato virus X genome. FEBS Lett, 213, 438-442.
106. Morozov S.Yu. and Solovyev A.G. (1999). Genome organization in RNA viruses. Molecular biology of plant viruses, pp. 47-98. Edited by C.L. Mandhar. Boston/Dordrecht/London: Kluwer
107. Morozov S.Yu, Dolja V.V. and Atabekov J.G. (1989). Probable reassortment of genomic elements among elongated RNA-containing plant viruses. JMolEvol, 29, 52-62.
108. Morozov S.Yu, Miroshnichenko N.A, Solovyev A.G, Fedorkin O.N, Zelenina D.A, Lukasheva L.I, Karasev A.V, Dolja V.V, Atabekov J.G. (1991). Expression strategy of the potato virus X triple gene block. J Gen Virol, 72,2039-2042.
109. Morozov S.Yu, Miroshnichenko N.A, Zelenina D.A, Fedorkin O.N, Solovijev A.G, Lukasheva L.I. and Atabekov J.C. (1990). Expression of RNA transcripts of potato virus X full-length and subgenomic cDNAs. Biochimie, 72, 677-684.
110. Morozov S.Yu, Solovyev A.G, Kalinina N.O, Fedorkin O.N, Samuilova O.V, Schiemann J, Atabekov J.G. (1999). Evidence for two nonoverlapping functional domains in the potato virus X 25K movement protein. Virology, 260(l):55-63.
111. Nebenfuhr A. (2002). Vesicle traffic in the endomembrane system: a tale of COPs, Rabs and SNAREs. Currt Opin Plant Biol, 13, 97-105.
112. Nicolas O, Dunnington S.W, Gotow L.F, Pirone T.P, Hellmann G.M. (1997). Variations in the VPg protein allow a potyvirus to overcome va gene resistance in tobacco. Virology, 237(2), 452-9.
113. Niesbach-Klosgen U„ Guilley H, Jonard G. and Richards K. (1990). Immunodetection in vivo of beet necrotic yellow vein virus-encoded proteins. Virology, 178, 52-61.
114. Ohno T, Takamatsu N, Meshi T, Okada Y, Nishiguchi M. and Kiho Y. (1983). Single amino acid substitution in 30K protein of TMV defective in virus transport function. Virology, 131, 255-258.
115. Okita T.W, Choi S.B. (2002). mRNA localization in plants: targeting to the cell's cortical region and beyond. Curr Opin Plant Bio, 5(6), 553-9.
116. Oparka K.J. (2004). Getting the message across: how do plant cells exchange macromolecular complexes? Trends Plant Sci, 9(1), 33-41.
117. Oparka K.J, Roberts A.G. (2001). Plasmodesmata. A not so open-and-shut case. Plant Physiol, 125(1), 3-6.
118. Oparka K.J, Roberts A.G, Roberts I.M, Prior D.A.M. and Santa Cruz S. (1996). Viral coat protein is targeted to, but does not gate, plasmodesmata during cell-to-cell movement of potato virus X. Plant J, 10, 805-813.
119. Д35. Pause A, Sonenberg N. (1992). Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J, 11(7), 2643-5.
120. Peremyslov V.V, Andreev I.A, Prokhnevsky A.I, Duncan G.H, Taliansky M.E, Dolja V.V. (2004). Complex molecular architecture of beet yellows virus particles. Proc Natl Acad Sci USA, 101, 5030-5035.
121. Petty I.T. and Jackson A.O. (1990). Mutational analysis of barley stripe mosaic virus RNA beta. Virology, 179, 712-718.
122. Petty I.T, French R, Jones R.W, Jackson A.O. (1990). Identification of barley stripe mosaic virus genes involved in viral RNA replication and systemic movement. EMBO J, 9(11), 3453-7.
123. Pilipenko E.V, Viktorova E.G., Guest S.T, Agol V.I. and Roos R.P.2001). Cell-specific proteins regulate viral RNA translation and virus-induced disease. EMBO J, 20, 6899-6908.
124. Ploubidou A. and Way M. (2001). Viral transport and the cytoskeleton. Curr Opin Cell Biol, 13, 97-105.
125. Prokhnevsky A.I, Peremyslov V.V, Dolja V.V. (2005). Actin cytoskeleton is involved in targeting of a viral Hsp70 homolog to the cell periphery. J Virol, 79, 14421-14428.
126. Prokhnevsky A.I, Peremyslov V.V, Napuli A.J. and Dolja V.V.2002). Interaction between long-distance transport factor and Hsp70-related movement protein of beet yellows virus. J Virol, 76, 11003-11011.
127. Rajamaki M.L. and Valkonen J.P. (1999). The 6K2 protein and the VPg of potato virus A are determinants of systemic infection in Nicandra physaloides. Mol Plant Microbe Interact, 12, 1074-1081.
128. Rajamaki M.L. and Valkonen J.P. (2002) Viral genome-linked protein (VPg) controls accumulation and phloem-loading of a potyvirus in inoculated potato leaves. Mol Plant Microbe Interact, 15, 138-149.
129. Rakitina DV, Kantidze OL, Leshchiner AD, Solovyev AG, Novikov VK, Morozov SY, Kalinina NO. (2005). Coat proteins of two filamentous plant viruses display NTPase activity in vitro. FEBS Lett, 579(22), 4955-60.
130. Revers F., Le Gall 0., Candresse T. and Maule A.J. (1999). New advances in understanding the molecular biology of plant/potyvirus interactions. Mol Plant Microbe Interact, 12, 367-376.
131. Roberts I.M., Wang D., Rudlay K. and Maule A.J. (1998). Ultrastructural and temporal observations of the potyvirus cylindrical inclusions (CIs) show that the CI protein acts transiently in aiding virus movement. Virology, 245,173-181.
132. Rodionova N.P., Karpova O.V., Kozlovsky S.V., Zayakina O.V., Arkhipenko M.V., Atabekov J.G. (2003). Linear remodeling of helical virus by movement protein binding. J Mol Biol, 333(3), 565-72.
133. Rodriguez-Cerezo E., Findlay K., Shaw J.G., Lomonossoff G.P., Qiu S.G., Linstead P., Shanks M. and Risco C. (1997). The coat and cylindrical inclusion proteins of a potyvirus are associated with connections between plant cells. Virology, 236, 296-306.
134. Rojas M.R., Murillo Zerbini F.M., Allison R.F., Gilbertson R.L., Lucas W.J. (1997). Capsid protein and helper component-proteinase function as potyvirus cell-to-cell movement proteins. Virology, 237, 283-295.
135. Roudet-Tavert G., German-Retana S., Delaunay T., Delecolle B., Candresse T., Le Gall O. (2002). Interaction between potyvirus helper component-proteinase and capsid protein in infected plants. J Gen Virol, 83, 1765-70.
136. Rouleau M., Smith R.J, Bancroft J.B. and Mackie G.A. (1994). Purification, properties, and subcellular localization of foxtail mosaic potexvirus 26-kDa protein. Virology, 204(1), 254-265.
137. Saito T, Yamanaka K. and Okada Y. (1990). Long-distance movementand virion assembly of tobacco mosaic virus mutants. Virology, 176, 329-336.
138. Sambrook J, Maniatis T. and Fritsch E.F. (1989). Molecular cloning: a laboratore manual. 2nd edn. New York, Cold Spring Harbor Laboratory.
139. Santa Cruz S, Roberts A.G, Prior D.A.M, Chapman S. and Oparka K.J. (1998). Cell-to-cell and phloem-mediated transport of potato virus X, the role of virions. Plant Cell, 10, 495-510.
140. Satyanarayana T, Gowda S, Ayllon M.A, Dawson W.O. (2004). Closterovirus bipolar virion: evidence for initiation of assembly by minor coat protein and its restriction to the genomic RNA 5 region. Proc Natl AcadSci USA, 101, 799-804.
141. Schaad M.C., Lellis A.D, Carrington J.C. (1997). VPg of tobacco etch potyvirus is a host genotype-specific determinant for long-distance movement. J Virol, 71, 8624-8631.
142. Schepetilnikov M.V, Manske U, Solovyev A.G, Zamyatnin A.A.Jr., Schiemann J, Morozov S.Y. (2005). The hydrophobic segment of Potato virus X TGBp3 is a major determinant of the protein intracellular trafficking. J Gen Virol, 86, 2379-91.
143. Schwartz M, Chen J, Janda M, Sullivan M, den Boon, J. and Ahlquist P. (2002). A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids. Mol Cell, 9, 505-514.
144. Schwer B. (2001). A new twist on RNA helicases: DExH/D box proteins as RNPases. Nat Struc Biol, 8, 113-116.
145. Serazev T.V, Kalinina N.O, Nadezhdina E.S, Shanina N.A, Morozov S.Y. (2003). Potato virus X coat protein interacts with microtubules in vitro. Cell Biol, 27(3), 271-2.
146. Shukla D.D, Strike P.M., Tracy S.L, Gough K.H., Ward C.M. (1988). The N and C termini of the coat proteins of potyviruses are surface-located and the N terminus contains major virus-specific epitopes. J Gen Virol, 69, 1497-1508.
147. Silhavy D, Molnar A, Lucioli A, Szittya G, Hornyik C, Tavazza M, Burgyan J. (2002). A viral protein suppresses RNA silencing and binds silencing-generated, 21- to 25-nucleotide double-stranded RNAs. EMBO J, 21(12), 3070-80.
148. Sit T.L. and Abouhaidar M.G. (1993). Infectious RNA transcripts derived from cloned cDNA of papaya mosaic virus: effect of mutations to the capsid and polymerase proteins. J Gen Virol, 74, 1133-1140.
149. Sodeik B. (2001). Mechanisms of viral transport in the cytoplasm. Trends Microbiol, 8(10), 465-72.
150. Solovyev A.G, Savenkov E.I, Grdzelishvili V.Z, Kalinina N.O, Morozov S.Yu, Schiemann J. and Atabekov J.G. (1999). Movement of hordeivirus hybrids with exchanges in the triple gene block. Virology, 253, 278-287.
151. Solovyev A.G., Stroganova T.A, Zamyatnin Jr.AA, Fedorkin O.N., Schiemann J. and Morozov S.Yu. (2000). Subcellular sorting of small membrane-associated triple gene block proteins, TGBp3-assisted targeting of TGBp2. Virology, 269(1), 113-127.
152. Soultanas P. and Wigley D.B. (2001). Unwinding the 'Gordian knot' ofhelicase action. Trends Biochem Set, 26, 47—54.
153. Soultanas P, Dillingham M.S., Velankar S.S, Wigley D.B. (1999). DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase. J Mol Biol, 290(1), 137-148.
154. Stephens D.J. and Pepperkok R. (2001). Illuminating the secretory pathway: when do we need vesicles 1J Cell Sci, 114, 1053-1059.
155. Subramanya H.S., Bird L.E., Brannigan J.A., Wigley D.B. (1996). Crystal structure of a DExx box DNA helicase. Nature, 384(6607), 379-83.
156. Tamai A. and Meshi T. (2001). Cell-to-cell movement of potato virus X: the role of p!2 and p8 encoded by the second and third open reading frames of the triple gene block. Mol Plant Microbe Interact, 14, 1158-1167.
157. Theis K, Chen P.J., Skorvaga M., Van Houten B., Kisker C. (1999). Crystal Structure of Uvrb, a DNA Helicase Adapted to Nucleotide Excision Repair. Embo J, 18, 6899-6907.
158. Torrance L., Andreev I.A., Gabrenaite-Verhovskaya R., Cowan G., Makinen K., Taliansky M.E. (2006). An unusual structure at one end of potato potyvirus particles. J Mol Biol, 357(1), 1-8.
159. Tseng S.S., Weaver P.L., Liu Y, Hitomi M, Tartakoff A. M. and Chang T.H. (1998). Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export. EMBO J, 17, 2651-2662.
160. Tzfira T, Rhee Y, Chen M.H., Kunik T., Citovsky V. (2000). Nucleic acid transport in plant-microbe interactions: the molecules that walk through the walls. Annu Rev Microbiol, 54, 187-219.
161. Urcuqui-Inchima S., Haenni A.-L., Bernardi F. (2001). Potyvirus proteins: a wealth of functions. Virus Res, 74, 157-175.
162. Van Lent J, Wellink J, Goldbach R. (1990). Evidence for the involvement of the 58K and 48K proteins in the intercellular movement of cowpea mosaic virus. J Gen Virol, 71, 219-223.
163. Vargason J.M., Szittya G., Burgyan J., Tanaka Hall T.M. (2003). Size selective recognition of siRNA by an RNA silencing suppressor. Cell, 115(7), 799-811.
164. Velankar S.S., Soultanas P., Dillingham M.S., Subramanya H.S., Wigley D.B. (1999). Crystal structures of complexes of PcrA DNA helicase with a DNA substrateindicate an inchworm mechanism. Cell, 97(1), 75-84.
165. Verchot J., Angell S.M. and Baulcombe D.C. (1998). In vivo translation of the triple gene block of potato virus X requires two subgenomic mRNAs. J Virol, 72(10), 8316-8320.
166. Verchot-Lubicz J. (2005). A new cell-to-cell transport model for Potexviruses. Mol Plant Microbe Interact, 18(4), 283-90.
167. Vetter I.R. and Wittinghofer A. (1999). Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer. Q Rev Biophys, 32(1), 1-56.
168. Voinnet O. (2001). RNA silencing as a plant immune system against viruses. Trends in Genetics, 17, 449-459.
169. Voinnet O., Lederer C. and Baulcombe D.C. (2000). A viral movement protein prevents spread of the gene silencing signal in Nicotiana benthamiana. Cell, 103, 157-167.
170. Walker J.E., Saraste M., Runswick M.J., Gay N.J. (1982). Distanly related sequences in the a- and P-subunits of ATP synthetase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold .EMBOJ, 1,945-951.
171. Wieczoreck A. and Sanfacon H. (1993) Characterization and subcellular localization of tomato ringspot nepovirus putative movement protein. Virology, 194, 732-742.
172. Wung C.H, Hsu Y.H., Liou D.Y., Huang W.C, Lin N.S. and Chang B.Y. (1999). Identification of the RNA-binding sites of the triple gene block protein 1 of bamboo mosaic potexvirus. J Gen Virol, 80, 1119-1126.
173. Xiong Z, Kim K.H, Giesman-Cookmeyer D. and Lommel S.A. (1993). The roles of the red clover necrotic mosaic virus capsid and cell-to-cell movement proteins in systemic infection. Virology, 192, 27-32.
174. Yang Y, Ding B, Baulcombe D.C, Verchot J. (2000). Cell-to-cell movement of the 25K protein of Potato virus X is regulated by three other viral proteins. Mol Plant Microbe Interact, 13, 599-605.
175. Yao N, Hesson T, Cable M, Hong Z, Kwong A.D, Le H.V, Weber P.C. (1997). Structure of the hepatitis C virus RNA helicase domain. Nat Struct Biol, 4, 463-467.
176. Yao N, Reichert P,Taremi S.S, Prosise W.W, Weber P.C. (1999). Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure FoldDes, 7, 1353-1363.
177. Ye K, Patel D.J. (2005). RNA silencing suppressor p21 of Beet yellows virus forms an RNA binding octameric ring structure. Structure, 13, 1375-1384.
178. Zheng H, Wang G, Zhang L. (1997). Alfalfa mosaic virus movement protein induces tubules in plant protoplasts. Mol Plant Microbe Interact, 10, 1010-1014.
179. Zhou H, Jackson A.O. (1996). Expression of the barley stripe mosaic virus RNAß "triple gene block". Virology, 216, 367-379.
180. Добров E.H, Немых M.A, Новиков B.K, Лукашина E.B, Баратова Л.А, Драчёв В.А., Ефимов A.B. (2006). ФИЗИКО-ХИМИЧЕСКИЕ ХАРАКТЕРИСТИКИ ВИРИОНОВ Х-ВИРУСА КАРТОФЕЛЯ И МОДИФИЦИРОВАННАЯ МОДЕЛЬ СТРУКТУРЫ ЕГО БЕЛКА ОБОЛОЧКИ. Молекулярная биология.
181. Калинина Н.О. (2003). Биохимические свойства белков, участвующих в образовании транспортных форм у некоторых РНК-содержащих вирусов растений. Диссертация на соискание ученой степени доктора биологических наук в виде научного доклада
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