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Структурно-функциональная характеристика гена рокристаллина лягушки Rana temporaria

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Компьютерный анализ структуры 5″ -участка гена р-кристаллина выявил гомологию с первичной структурой промоторного участка гена карбомил фосфат синтетазы-1 Rana catesbeiana, а также наличие ряда регуляторных элементов, характерных для промоторов других кристаллиновых генов. Сконструирована представительная кДНК библиотека на матрице мРНК из хрусталика лягушки R. temporaria. Идентифицирован клон… Читать ещё >

Содержание

  • 3. 1. Введение
  • 3. 2. ТКАНЕСПЕЦИФИЧЕСКАЯ ЭКСПРЕССИЯ р-КРИСТАЛЛИНА
  • 3. 3. Получение полноразмерной кДНК р-кристаллина хрусталика глаза лягушки Rana temporaria
    • 3. 3. 1. Получение и скрининг библиотеки кДНК из хрусталика глаза лягушки Rana temporaria
  • 3. 4. Получение и скрининг геномного банка травяной лягушки Rana temporaria
    • 3. 4. 1. Получение банка хромосомной ДНК лягушки R. temporaria
    • 3. 4. 2. Скрининг геномного банка
  • 3. 5. Анализ клонов и построение рестрикционных карт
  • 3. 6. Экзон-Интронная структура ДНК геномных клонов
  • 3. 7. Идентификация промоторного участка гена р-кристаллина лягушки Rana temporaria
  • 4. ОБСУЖДЕНИЕ РЕЗУЛЬТАТОВ
  • ВЫВОДЫ
  • Структурно-функциональная характеристика гена рокристаллина лягушки Rana temporaria (реферат, курсовая, диплом, контрольная)

    5 ВЫВОДЫ.

    1. Впервые получены доказательства хрусталикоспецифической экспрессии гена ро-кристаллина лягушки R. temporaria.

    2. Сконструирована представительная кДНК библиотека на матрице мРНК из хрусталика лягушки R. temporaria. Идентифицирован клон, несущий полноразмерную последовательность кДНК р-кристаллина, и определена его первичная структура.

    3. Создан геномный банк лягушки R. temporaria, из которого с помощью кДНК-зонда выделены клоны, содержащие участки гена р-кристаллина.

    4. Построена детальная рестрикционная карта полученных геномных клонов.

    5. Проведена структурная характеристика геномных клонов. Доказано наличие в геноме лягушки по крайней мере четырех копий гена р-кристаллина, один из которых вероятно является псевдогеном.

    6. Впервые идентифицирован и структурно охарактеризован геномный клон, содержащий 5'концевой участок гена р-кристаллина, который по совокупности данных может содержать промотор гена р-кристаллина.

    7. Компьютерный анализ структуры 5″ -участка гена р-кристаллина выявил гомологию с первичной структурой промоторного участка гена карбомил фосфат синтетазы-1 Rana catesbeiana, а также наличие ряда регуляторных элементов, характерных для промоторов других кристаллиновых генов.

    1. Маниатис, Э. Фрич, Дж. Сэмбрук. Молекулярное клонирование.// Мир, Москва. 1984.

    2. Князева М. В., Афторефера кандидатской диссертации, М, 1990.

    3. Долгилевич С. М., Снеговая И. Ю., Микаелян А. С. Таксоноспецифический белок хрусталика глаза лягушки: филогенетическое родство с белками семейства NADP-зависимых редуктаз., ДАН, серия биология, 1994, № 4, ст. 577−587.

    4. Aarts H.J., Lubsen N.H., and Schoenmakers J.G. Crystallin gene expression during rat lens development. // Eur. J. Biochem. 1989. V. 183. P. 31−38.

    5. Alemany J., Borras Т., and de Pablo J. Transcriptional stimulation of the deltal-crystallin gene by insulin-like growth factor I and insulin requires DNA cis elements in chicken. // Proc. Natl. Acad. Sci. USA. 1990. V. 87. P. 33 533 359.

    6. Agata K., Yasuda K., and Okada T.S. Gene coding for a lens-specific protein, delta-crystallin, is transcribed in nonlens tissues of chicken embryos. // Dev. Biol. 1983. V. 100. P. 222−228.

    7. Bagby S., Harvey T.S., EagleS.G., Inouye S., and Ikura M. NMR-derived three-dimensional solution structure of protein S complexed with calcium// Structure. 1994a. V. 2. P. 107−122.

    8. Barbosa P., Cialkowsky M., and o’Brien W.E. Analysis of naturally occurring and site directed mutations in the argininosuccinate lyase gene. // J.Biol. Chem. 1991a. V. 266. P. 5286−5290.

    9. Barnstable C.J. Glutamate and GABA in retinal circuitry. // Cur. Opinion Beurobiol. 1993. B. 3. P. 520−525.

    10. Bax G., Lapatto R., Nalini V., Driessen H., Lindley P.F., Mahadevan D., Blundell T.L., and Slingsby C. X-ray analysis of bettaB2-crystallin and evolution of oligomeric lens proteins. // Nature. 1990. V. 347. P. 776−780.

    11. Berbers G.A., Hoekman W.W., Kleinschmidt T., and Braunitzer G. Homology between the primary structures of the major bovine betta-crystallin chains. // Eur. J. Biochem. 1984. V. 139. P. 467−479.

    12. Bhat S.P. and Nagineni C.N. alphaB-Subunit of lens specific protein alpha-crystallin is in other ocular and non ocular tissues. // Biochem.Biophys. Res. Commun. 1989. V. 158. P. 319−323.

    13. Bloemendal, H., Molecular and Cellular Biology of the Eye Lens. 1981. Willey, New York.

    14. Blundell T.K., Lindley P., Miller L., Moss D., Slingsby C., Tickle I., Turnell B., and Wistow G. The molecular structure and stability of the eye lens: x-ray analysis of gamma-crystallinll. // Nature. 1981. V. 289. P. 771−777.

    15. Bohren K.M., Bullock B., Wermuth B., and Gabbay K.H. The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.// J. Biol. Chem. 1989. V. 264. P. 9547−9551.

    16. Borras T., Nickerson J.M., and Chepelinsky A.B. Structural and functional evidence for differential promoter activity of the two linked delta-crystallin genes in the chicken. // EMBO J. 1985. V. 4. P. 445−448.

    17. Borras T., Persson B., and Jornvall H. Eye lens dzetta-crystallin: relationships to the family of long-chain alcohol/polyol dehydrogenases. // Biochem. 1989. V. 28. P. 6133−6139.

    18. Borras T., Peterson C.A. and Piatigorsky J. Evidence for posititve and negative regulation in the promoter of the chicken deltal-crystallin gene. // Dev. Biol. 1988. V. 127. P. 209−215.

    19. Brakenhow R.H., Arts H.J., Reek F.H., Lubsen N.H., and Schoenmakers J.G. Human gamma-crystallin genes. A gene family on its way to extinction. // J. Mol. Biol. 1990. V. 216. P. 519−532.

    20. Breitman M.L., Clapoff S., and Rossnat J. Genetic ablation: Targeted expression of atoxin gene causes microphthalmia in transgenic mice. // Science. 1987. V. 238. P. 1563−1571.

    21. Carper D., Nishimura C., Shinohara T., Dietzschold B., Wistow G., Craft C., Kador P., and Kinoshita J.H. Aldose reductase and hj-crystallin belong to the same protein superfamily as aldehyde reductase. // FEBS Letters. 1987. V. 220. P. 209−213.

    22. Carper D.A., Wistow G., Nishimura C., Graham C., Watanabe K., Fujii Y., a.

    23. Hayashi H., and Hayaishi O. A superfamily of NADPH-dependent reductases in eukaryotes and prokaryotes. // Exp. Eye Res. 1989. V. 49. P. 377−388.

    24. Chepelinsky A.B., Sommer B., and Piatigorsky J. Interaction between two different regulatory elements activates the murine alphaA-crystallin gene promoter in explanted lens epithelia. // Mol. Cell Biol. 1987. V. 7. P. 18 071 812.

    25. Chiesa R., Gawinowicz-Kolks M.A., Kleiman N.J., and Spector A. The phosphorylation sites of the B2 chain of bovine alpha-crystallin. // J.Biol. Chem. 1987. V. 144. P. 1340−1347.

    26. Chiesa R., Gawinowicz-Kolks M.A., and Spector A. The phosphorylation of the primary gene products of alpha-crystallin. // J. Biol. Chem. 1987. V. 262. P. 1438−1441.

    27. Chiesi M., Longoni S., and Limbruno U. Cardiac alpha-crystallin. III. Involvement during heart ischemia. // Mol. Cel. Biochem. 1990. V. 97. P. 129−136.

    28. Chiou S.H. A novel crystallin from octopus lens. // FEBS Letters. 1988. V 241. P. 261−264.

    29. Clayton R.M., Jeanny J.C., and Bower D.J. The presence of exptralenticular crystallins and its relationship eith transdifferentiation to lens. // Curr. Top Dev. Biol. 1986. V. 20. P. 137−144.

    30. Cvekl A. and Piatigorsky J. Lens development and crystallin gene expression: many roles for Pax-6. // BioEssays. 1996. V. 18. N. 8. P. 621 631.

    31. Cvekl A., Sax C.M., Li X., McDermott J.B., and Piatigorsky J. Pax-6 and lens-specific transcription of the chicken deltal-crystallin gene. // Proc. Natl. Acad. Sci. USA. 1995. V. 92. P. 4681−4685.

    32. Das G.C. and Piatigorsky J. The chicken deltal-crystallin gene promoter: Binding of transcription factor (s) to the upstream G + C-rich region is necessary for promoter function in vitro. // Proc. Natl. Acad. Sci. USA. 1986. V. 83. P. 3131−3137.

    33. Das G.C. and Piatigorsky J. Promoter activity of the two chicken delta-crystallin genes in HeLa cell extract. // Curr. Eye Res. 1988. V. 7. P. 331 337.

    34. Dasgupta S., Hohman T.C., and Carper D. Hypertonic stress induces alphaB-crystallin expression. // Exp. eye Res. 1992. V. 54. P. 461−468.

    35. Dorn A., Affolter M., Gehring W., and Leupin W. Homeodomain pro-teins in development and therapy. // Pharmac. Ther. 1994. V. 61. P. 155−183.

    36. Driessen H.P., Herbrink P., Bloemendal H., and de Jong W.W. The betta-crystallin Bp chain is internally duplicated and homologous gamma-crystallin. // Exp. Eye Res. 1980. V. 31. P. 243−246.

    37. Dubin R.A., Wawrousek E.F., Piatigorsky J. Expression of the murine alphaB-crystallin gene is not restircted to the lens. // Mol. Cell. Biol. 1989. V. 9. P. 1083−1091.

    38. Duncan M.K., Li X., Ogino H., Yasuda K., and Piatigorsky J. Developmental regulation of the chicken bettaBl-crystallin promoter in transgenic mice. // Mech. Dev. 1997.

    39. Flaherty R.M., McKay D.B., Kabsch W., and Holmes K.C. Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70kDa heat shock cognate protein. // Proc. Natl. Acad. Sci. USA. 1991. V. 88. P. 5041−5045.

    40. Gao, C.Y., Bassnett, S., and Zelenka, P. S. Cyclin B, p34cdc2 and Hl-kinase actitity in terminally differentiating lens fiber cells. 1994.

    41. Garland D., Rao P.V., Del Corso A., Mura U., and Zigler J.S. Dzetta-Crystallin is a major protein in the lens of Camelus dromedarius. // Arch. Biochem. Biophys. 1991. V. 285. P. 134−136.

    42. Goto K., Okada T.S., and Kondoh H. Functional cooperation of lens specific and hohspecific elements in the delta 1-crystallin enhancer. // Mol. Cell Biol. 1990. V. 10. P. 958−961.

    43. Graham C., Szpirer C., Levan G., and Carper D. Characterizati-on of the adlose reductase-encoding gene family in rat. // Gene. 1991. V. 107. P. 259 267.

    44. Harding J.J. and Crabbe M.J.C. The lens: development, proteins, metabolism and cataract. // The Eye. Vol. IB. H. Davson, Eds. 1984. Academic Press, New York. P. 207−492.

    45. Hartl F.U., Hlodan R., and Langer T. Molecular chaperones in protein folding: the art of avoiding sticky situations. // Trends Biochem. Sci. 1994. V. 19. P. 20−25.

    46. Hayashi S., Goto K., and Okada T.S. Lens-specific enhancer in the third intorn regulates espression of the chicken deltal-crystallin gene. // Genes Dev. 1987. V. 1. P. 818−822.

    47. Hayashi S. and Kondoh H. In vivo competition of delta-crystallin gene expression by DNA fragments containing a GC box. // Mol. Cell. Biol. 1986. V. 6. P. 4130−4138.

    48. Hayashi S., Kondoh H., and Yasuda K. Tissue-specific regulation of a chicken delta-cryatallin gene in mouse cells: Involvement of the 5' end region. // EMBO J. 1985. V. 4. P. 2201−2207.

    49. Haynes J.I., Duncan M.K., and Piatigorsky J. Spatial and tem-poral activity of the alphaB-crystallin/small heat shock protein gene promoter in transgenic mice. // Dev. Dynam. 1996.

    50. Hejtmancik J.F., Beebe D.C., and Ostrer H. delta and betta-Crystallin mRNA levels in the embryonic and posthatched chicken lens: Temporal and skpatial changes during development. // Dev. Biol. 1985. V. 109. P. 72−76.

    51. Hejtmancik J.F. and Piatigorsky J. Molecular biology of the lens. //In: Albert&Jakobiec: Principles and practice of ophthalmology. W.B. Saunders Company., 1994, p. 169−181.

    52. Hogg D., Tsui L.C., and Gorin M. Characterization of the human betta-crystallin gene Hu bettaA3/Al reveals ancestral relationships among the betta-gamma-crystallin superfamily. // J. Biol. Chem. 1986. V. 261. P. 12 420−12 425.

    53. Horwitz J. A-Crystallin can function as a molecular chaperone. // Proc. Natl. Acad. Sci. USA. 1992. V. 89. P. 10 449−10 453.

    54. Horwitz J. The junction of alpha-crystallin. // Proctor Lecture Invest, ophthalmol. Vis. Sci. 1995. P. 35−41.

    55. Huang W.L., Russell P., Stone S., and Zigler J.S. dzetta-Crystallin, a novel lens protein from the guinea pig. // Cur. Eye Res. V. 6. P. 725−732.

    56. Inana G., Piatigorsky J. Norman B. Gene and protein structure of a betta-crystallin polypeptide in murine lens: Relationship of exons and structural motifs. // Nature. 1983. V. 302. P. 310−314.

    57. Ingolia T.D. and Craig E.A. Four small Drosophila heat shock proteins are related to mammalian alpha-crystallin. // Proc. Natl. Acad. Sci. USA. 1982. V. 79. P. 2360−2369.

    58. Inoue K., Ozato K., and Kondoh H. Stage-dependent expression of the chicken delta-cryatallin gene in transgenic fish embryos. // Cell Differ. Dev. 1989. V. 27. P. 57−61.

    59. Jahn D., Verkamp E., and Soil D. Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis. // Trends Biochem. Sci. 1992. V. 17. P. 215−218.

    60. Kantorow M. and Piatigorsky J. alpha-Crystallin/small heat shock protein has autokinase activity. // Proc. Natl. Acad. Sci. USA. V. 91. P. 3112−3116.

    61. Kato K., Shinohara H., Kurobe N. Immunoreactive alphaA-crystallin in rat non-lenticular tissues letected with a sensitive immunoassay method. // Biochim. Biophys. Acta. 1991. V. 1080. P.173−179.

    62. Kim R.Y., Gasser R., and Wistow G.J. mu-Crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina. // Proc. Natl. Acad. Sei. USA. 1992. V. 89. P. 9292−9296.

    63. King C.R. and Piatigorsky J. Alternative RNA splicing of the murine alphaA-crystallin gene: Protein-coding information within an intorn. // Cell. 1983. V. 32. P. 707−711.

    64. Kinoshita J.H., Datiles M.B., Kador P.F., and Robinson W.G. Aldose reductase and diabetic eye complications. // Rifkin H. and Por-te D., Eds. Diabetes Mellitus. Theory and Practice. 4th ed., Elsevier, New York, 1990. P. 264−278.

    65. Klement J.J., Wawrousek E.F., and Piatigorsky J. Tissue-specific expression of the chicken alphaA-crystallin gene in cultured lens epithelia adn transgenic mice. // J. Biol. Chem. 1989. V. 264. P. 19 837−19 842.

    66. Kiemenz R., Frohli E., Steiger R.H., Schafter R., and Aoyama A. alphaB-Crystallin is a small heat shock protein. // Proc. Natl. Acad. Sei. USA. 1991b. V. 88. P. 3652−3656.

    67. Komori N., Usukura J., and Matsumoto H. Drosocrystallin, a major 52 kDa glycoprotein of the Drosophila melanogaster corneal lens. Purification, biochemical characterization and subcellular localization. // J. Cell Sci. 1992. V. 102. P. 191−201.

    68. Kondoh H., Katoh K., Takahashi Y. Developmental regulation of the chicken delta 1-crystallin gene: Analysis by transgenesis and gene dissection. // Cell Differ. Dev. 1988. V. 25. P. 53−59.

    69. Kondoh H., Araki I., Yasuda K., Matsubasa T., and Mori M. Expression of the chicken delta-crystallin gene in mouse cells: evidence for encoding of argininosuccinate lyase. // Gene. 1991. V. 99. P. 267−271.

    70. Kondoh H., Yasuda K., and Okada T.S. Tissue-specific expression of a cloned chick delta-crystallin gene in mouse cells. // Nature. 1983. V. 301. P. 440−447.

    71. Li X., Wistow G.J. and Piatigorsky J. Linkage and expression of the argininosuccinate lyase/delta-crystallin genes of the duck: insertion of a CR1 element in the intragenic spacer. // Biochim. Biophys. Acta. 1994.

    72. Lok S., Breitman M.L., Chepelinsky A.B. Lens-specific promoter activity of a mouse gamma-crystallin gene. // Mol. Cell Biol. 1985. V. 5. P. 2221−2228.

    73. Lok S., Stevens W., and Breitman M.L. Multiple regulatory elements of the murine gamma2-crystallin promoter. // Nucleic Acids Res. 1989. V. 17. P. 3563−3569.

    74. Matsuo I., Kitamura M., Okazaki K., and Yasuda K. Binding of a factor to an enhancer element responsible for the tissue specific expression of the chicken alphaA-crystallin gene. // Development. 1991. V. 113. P. 539−545.

    75. McDermott J.B., Cvekl A., and Piatigorsky J. Lens-specific expression of chicken bettaA3/Al crystallin promoter fragment in transgenic mice. // Biochem. Biophys Res. Commun. 1996. V. 221. P. 559−564.

    76. Meakin S.O., Breitman M.L., Tsui L.C. Structural and evolutionary relationships among five members of the human gamma-crystallin gene family. // Mol. Cell Biol. 1985. V. 5. P. 1408−1412.

    77. Meakin S.O., Du R.P., Tsui L.C. gfvvf-Crystallins of the human eye lens: Expression analysis of five members of the gene family. // Mol. Cell Biol. 1987.V. 7. P. 2671−2683.

    78. Milstone L.M., Zelenka P., and Piatigorsky J. delta-Crystallin mRNA in chick lens cells: mRNA accumulates during defferential stimulation of delta-crystallin synthsis in cultured cells. // Dev. Biol. 1976. V. 48. P. 197−202.

    79. Miron T., Vancompernolle K., Vandekerckhove J., Wilchek M., and Geiger B. A 25kD inhibitor of actin polymerization is a low molecular mass heat shock protein. // J. Cel. Biol. 1991. V. 114. P. 255−261.

    80. Moormann R. J.M., den Dunnen J.T., and Bloemendal H. Extensive intragenic sequence homology in two distinct rat lens gamma-crystallin cDNAs suggests dublications of a primordial gene. // Proc. Natl. Acad. Sci. USA. 1982. V. 79. P. 6876−6880.

    81. Mulders J.W., Hendriks W., Blankesheijn /w.M., Bloemendal H., and de Jong W.W. lambda-Crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases. // J. Biol. Chem. 1988. V. 263. P. 15 462−15 466.

    82. Murer-Orlando M., Paterson R.C., and Lok S. Differential regulation of gamma-crystallin genes during mouse lens development. // Dev. Biol. 1987. V. 119. P. 260−267.

    83. Nicholl I.D. and Quinlan R.A. Chaperone activity of alpha-crystallins modulates intermediate filament assembly. // EMBO J. 1994. V. 13. P. 945 953.

    84. Nickerson J.M., Wawrousek E.F., and Borras T. Sequence of the chicken delta2-crystallin gene and its intergenic spacer: Extreme homology with the delta 1-ciystallin gene. //J. Biol. Chem. 1986. V. 261. P. 552−559.

    85. Nickerson J.M., Wawrousek E.F., Hawkins J.W., Wakil A.S., Wistow G.J., Thomas G., Norman B.L., and Piatigorsky J. The complete sequence of the chicken delta 1-crystallin gene and its flanking region. // J. Biol. Chem. 1985. V. 260. P. 9100−9105.

    86. Nickerson J.M., Wawrousek E.F., Borras T., Hawkins J.W., Norman B.L., Filpula D.R., Nagle J.W., Ally A.H., and Piatigorsky J. Sequence of the chicken delta 1 crystallin gene. // J. Biol. Chem. 1986. V. 261. P. 552−557.

    87. Ostrer H. and Piatigorsky J. betta-Crystallins of the adult chicken lens: relatedness of the polypeptides and their aggregates. // Exp. Eye Res. 1980. V. 30. P. 679−689.

    88. Parker D.S., Wawrouser E.F., and Piatigorsky J. Expression of the delta-crystallin genes in the embryonic chicken lens. // Dev. Biol. 1988. V. 126. P. 375−381.

    89. Peek R., van der Logt P., and Lubsen N.H. Tissueand species-specific promoter elements of rat gamma-crystallin genes. // Nucleir Acids Res. 1990. V. 18. P. 1189−1192.

    90. Peterson C.A. and Piatigorsky J. Preferential conservation of the glogular domains of the bettaA3/Al-crystallin polypeptide of the chiken eye lens. // Gene. 1986.

    91. Piatigorsky, J. Lens differentiation in vertebrates. A review of cellular and molecular features. // Differentiation. 1981. V. 119. P. 363−375.

    92. Piatigorsky J. Delta-Crystallin and their nucleic acids. // Mol. Cel. Biochem. 1984. V. 59. P. 33−56.

    93. Piatigorsky J., O’Brien W.E., Norman B.L., Kalumuk K., Wistow G.J., Borras T., Nickerson J.M., and Wawrousek E.F. Gene sharing by delta-crystallin and argininosuccinate lyase. // Proc. Natl. Acad. Sci. USA. 1988. V. 85. P. 3479−3483.

    94. Piatigorsky J., Horwitz J., Kuwabara T., and Cutress C.E. The cellular eye lens and crystallins of cubomedusan jellyfish. // J. Compar. Phys. A. 1989. V. 164. P. 577−587.

    95. Piatigorsky J. and Zelenka P. S. Transcriptional regulation of crystallin genes: cis-elements, trans-factors, and signal transduction systems in the lens. // Adv. Dev. Biochem. 1992. V. 1. P. 211−256.

    96. Quax-Jeuken Y., Driessen H., and Leunissen J. bettas-Crystallin: Structure and evolution of a distinct member of the bettagamma-superfamily. // EMBO J. 1985a. V. 4. P. 2597−2603.

    97. Quax-Jeuken Y., Quax W., Van Rens G. Complete structure of the alphaB-crystllin gene: Conservation of the exon-intron distribution in the two nonlinked alpha-crystallin genes. // Proc. Natl. Acad. Sci. USA. 1985. V. 82. P. 5819−5825.

    98. Rao G.N. and Cotlier E. Urea cycle enzymes in retina, ciliary body-iris, lens nad senile cataracts. // Exp. Eye Res. 1984. V. 39. P. 483−459.

    99. Rao P.V., Krishna C.M., and Zigler J.S. Identification and characterization of the enzymatic activity of dzetta-crystallin from guinea pig lens. A novel NADPH: quinone oxidoreductase. // J. Biol. Chem. 1992. V. 267. P. 96−102.

    100. Rodokanaki a., Holmes R.K., and Borras T. Dzetta-Crystallin, a novel protein from the guinea pig lens is related to alcohol dehydrogenases. // Gene. 1989. V. 78. P. 215−224.

    101. Roquemore E.P. Dell A., Morris H.R., Panico M. Reason A.J., Savoy L.-A., Wistow G.J., Zigler J.S., Earles B.J., and Hart G.W. Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine. // J. Biol. Chem. 1992. V. 267. P. 555−563.

    102. Roth H.J., Das G.C., and Piatigorsky J. Chicken bettaBl-crystallin gene expression: Presence of conserved functional polyoma enhancer-like andoctomer binding-like promoter elements found in non-lens genes. // Mol. Cell Biol. 1991. V. 11. P. 1488−1492.

    103. Rudner G., Katar M., and Maisel H. Enolase in the avian and turtle lens. // Cur. Eye Res. 1990. V. 9. P. 139−150.

    104. Russell P., Meakin S.O., Hohman T.C., Tsui L.C., and Breitman M.L. Relationship between proteins encode by three human gamma-crystallin genes and distinct polypeptides in the eye lens. // Mol. Cel. Biol. 1987. V. 7. P. 3320−3323.

    105. Sans N., Schindler U., and Schroder J. Ornithine cyclodeaminase from Ti plasmid C58: DNA sequecne, enzyme properties and regulation of activity by arginine. // Eur. J. Biochem. 1988. V. 173. P. 123−130.

    106. Sax C.M., Farrell F.X., Zehner Z.E. Regulation of vimentin gene expression in the ocular lens. // Dev. Biol. 1990. V. 139. P. 56−62.

    107. Sax C.M. and Piatigorsky J. Expression of the alpha-crystal-lin/small heat shock protein/molecular chaperone genes in the lens and other tissues. // Adv. Enzymol. Relat. Areas Mol. Biol. 1994. V. 69. P. 155−201.

    108. Sekido R. The delta-crystallin enhancerbinding protein del-taEFl is a repressor of E2-box-mediated gene activation. // Mol. Cell. Biol. 1994. V. 14. P. 5692−5700.

    109. Smolich B.D., Tarkington S.K., Saha M.S., and Grainger R.M. Xenopus gamma-crystallin gene expression: Evidence that the gamma-crystallin gene family is transcribed in lens and non-lens tissues. // Mol. Cel. Biol. 1994. V. 14. P. 1355−1363.

    110. Stapel S.O. and de Jong W.W. Lamprey 48 rDa lens protein represents a novel class of crystallins. // FEBS Lett. 1983. V. 162. P. 305−309.

    111. Stapel S.O., Zzweers A., Dodemont H.J., Kan J.H., and de Jong W.W. Epsylon-crystallin, a novel avian and reptilian eye lens protein. // Eur. J. Biochem. 1985. V. 147. P. 129−136.

    112. Sullivan C.H., Norman J.T., and Borras T. Developmental regulation of hypomethylation of delta-crystallin genes in chicken embryo lens cells. // Mol. Cell Biol. 1989. P. 3132−3136.

    113. Takahashi Y., Hanaoka K., and Hayasaka M. Embryonic stem cell-mediated transfer and correct regulation of the chicken delta-crystallin gene in developing mouse embryos. // Development. 1988. V. 102. P. 259−265.

    114. Thomas G., Zelenka P. S., and Cuthbertson R.A. Differential expression of the two delta-crystallin/argininsuccinate lyase genes in the lens, heart and brain of the chicken embryo. // New Biol. 1990. V. 2. P. 903−911.

    115. Thompson M.A., Hawkins J.W., and Piatigorsky J. Complete nucleotide sequence of the chicken alphaA-crystallin gene and its 5'-flanking region. // Gene. 1987. V. 56. P. 173−179.

    116. Thomson I., Wilkinson C.E., and Jackson J.F. Isolation and cell-free translation of chick lens crystallin mRNA during normal development and transdifferentiation of neural retina. // Dev. Biol. 1978. V. 65. P. 372−377.

    117. Tomarev S.I., Sundin O., Baneijee-Basu S., Duncan M.K., Yang J.-M., and Piatigorsky J. Chicken homeobox gene Prox 1 relatyed to Drosophila prospero is expressed in the developing lens and retina. // Dev. Dynamics. 1996. V. 206. P. 354−367.

    118. Tomarev S.I. and Zinovieva R.D. Squid major lens polypeptides are homologous to glutathione S-transferases subunits // Nature. 1988. V. 336. P. 86−88.

    119. Tomarev S.I., Zinovieva R.D., and Piatigorsky J. Crystallins of the octopus lens. Recruitment from detoxification enzymes. // J. Biol. Chem. 1991. V. 266. P. 24 226−24 231.

    120. Tomarev S.I., Zinovieva R.D., and Piatigorsky J. Characteriza-tion of Squid Crystallin Genes. // J. Biol. Chem. 1992. V. 267. N. 12. P. 8604−8612.

    121. Tomarev S.I., Chung S., Zinovieva R.D., and Piatigorsky J. Structure and in vitor expression of S-crystallins and gluthathione S-transferases of the squid. // Inv. Ophthalmol. Vis. Sci. 1994. V. 35. P. 1997;2003.

    122. Treton J.A., Jones R.E., King C.R., and Piatigorsky J. Evidence against gamma-crystallin DNA or RNA sequences in the chick. Exp. Eye Res. 1984. V.39. P. 513−522.

    123. Voorter C.E.M., Mulders J.W.M., Bloemendal H., and de Jong W.W. Some aspects of the phosphorylation of alpha-crystallin A // Eur. J. Biochem. 1986. V. 160. P. 203−210.

    124. Voorter C.E., de Haard-Hoekman W.A., Roersma E.S., Meyer H.E., Bloemendal H., and de Jong W.W. The in vivo phosphorylation sites of bovine alphaB-crystallin. // FEBS Let. 1989. V. 259. P. 50−52.

    125. Wawrousek E.J., Chepelinsky A.B., and McDermott J.B. Regulation of the murine alphaA-crystallin promoter in transgenic mice. // Dev. Biol. 1990. V. 137. P. 68−73.

    126. Weiner H. Enzymology and Molecular Biology of Carbonyl Metabolism. 3rd edn. 1990. Plenum Press. New York.

    127. Williams K.R., Reddigari S., and Patel G.L. Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5. // Proc. Natl. Acad. Sci. USA. 1985. V. 82. P. 5260−5264.

    128. Wistow G. Domain structure and evolution in alpha-crystallins and small heat-shock proteins. // FEBS Lett. 1985. V. 181. P. 1−15.

    129. Wistow G. Evolution of a protein superfamily: relationships between vertebrate lens crystallins and micro-organism dormancy proteins. // J. Mol. Evol. 1990. V. 30. P. 140−145.

    130. Wistow, G. Lens crystallins: gene recruitment and evolutionary dynamism. // Trends in Biochemical Science. 1993b. V. 18. P. 301−306.

    131. Wistow G. Possible tetramer-based quaternary structures for alpha-crystallins and small heat shock proteins. // Exp. Eye Res. 1993c. V. 56. P. 729−732.

    132. Wistow G., Anderson A., and Piatigorsky J. Evidence for neutral and selective processes in the recruitment of enzyme-crystallins in avian lenses. // Proc. Natl. Acad. Sci. USA. 1990. V. 87. P. 6277−6280.

    133. Wistow G. adn Kim H. Lens protein expression in mammals: taxon-specificity and the recruitment of crystallins. J. Mol. Evol. 1991. V. 32. P. 262−269.

    134. Wistow G.J., Lietman T., Williams L.A., Stapel S.O., de Jong W.W., Horwitz J., and Piatigorsky J. Teta-cryatallin/alpha-enolase: One gene encodes both an enzyme and a lens structural protein. // J. Cell Biol. 1988. V. 107. P. 2729−2736.

    135. Wistow G.J., Mulders J.W., and de Jong W.W. The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses. // Nature. 1987. V. 326. P. 622−624.

    136. Wistow G. and Piatigorsky J. Recruitment of enzymes as lens structural proteins. // Science. 1987. V. 236. P. 1554−1556.

    137. Wistow G. and Piatigorsky J. Lens crystallins: evolution and expression of proteins for a highly specialized tissue. // Ann. Rev. Biochem. 1988. V. 57. P. 479−504.

    138. Wistow G. and Piatigorsky J. Gene conversion and splice-site slippage in the argininosuccinate lyases/delta-crystallins of the duck lens: members of an enzyme superfamily. // Gene. 1990. V. 96. P. 263−270.

    139. Wistow G., Richardson J., Jaworski C., Graham C., Sharon-Friling R., and Segovia L. Crystallins: the over-expression of functional enzymes and stress proteins in the eye lens. // Biotechnology and Genetic Engineering Reviews. 1994. V. 12. P. 1−38.

    140. Wistow G. and Segovia L. mu-Crystallin: and unexpected marker for photoreceptors. // Inv. Ophthalmol. Visual Sci. 1994. V. 35. P. 2073.

    141. Wistow G., Slingsby C., Blundell T., Driessen H., de Jong W., and Bloemendal H. Eye-lens proteins: the three-dimensional strucutre of betta-crystallin predicted from monomelic gamma-crystallin. // FEBS Let. 1981. V. 133. P. 9−16.

    142. Wistow G. Summers L., and Blundell T. Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens betta-gamma-crystallins. // Nature. 1985. V. 315. P. 771−773.

    143. Wistow G., Turnell B., Summers L., Slingsby C., Moss D., Miller L., Lindley P., and Blundell T. X-ray analysis of the eye lens protein gamma-II crystallin at 1.9 A resolution. // J. Mol. Biol. 1983. V. 170. P. 175−202,.

    144. Yamada Y., Nakamura T., and Westphal H. Synthsis of alpha-crystallin by a cell line derived from the lens of a transgenic animal. // Curr. eye Res. 1990. V. 9. P. 31−39.

    145. Yasuda K. and Okada T.S. Structure and expression of chicken crystallin genes. // zoxf. Surv. Eukaryot. Genes. 1986. V. 3. P. 183−188.

    146. Yu C.C.-K., Tsui L.-C., and Breitman M.L. Homologous and heterologous enhancers modulate spatial expression but not cell-type specificity of the murine gamma-crystallin promoter. // Development. 1990. V. 110. P. 131 136.

    147. Zelenka P. S. and Piatigorsky J. Isolation and in vitor translation of delta-crystallin mRNA from embryonic chick lens fibers. // Proc. Natl. Acad. Sci. USA. 1974. V. 71. P. 1896−1899.

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