RAD51

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/RAD51 latin yazuında])
Навигациягә күчү Эзләүгә күчү
RAD51
Нинди таксонда бар акыллы кеше[d][1]
Кодирующий ген RAD51[d][1]
Молекулярная функция нуклеотид-связывающий[d][2][2], ДНК-связывающий[d][2][2], ATP-dependent activity, acting on DNA[d][3], DNA strand exchange activity[d][2][4], DNA polymerase binding[d][5], protein C-terminus binding[d][6], связывание с белками плазмы[d][7][8][9][…], four-way junction DNA binding[d][3], связывание похожих белков[d][9][10][11][…], endodeoxyribonuclease activity[d][3], АТФ-связанные[d][2][2][12], single-stranded DNA binding[d][13][3][14], double-stranded DNA binding[d][13][3][14], single-stranded DNA helicase activity[d][15][16][17], chromatin binding[d][18], double-stranded DNA binding[d][15][2][16][…], single-stranded DNA binding[d][15][2][16][…], ATP-dependent activity, acting on DNA[d][2][4] һәм enzyme binding[d][18]
Күзәнәк компоненты Цитоплазма[2][15][19][…], site of double-strand break[d][20], PML body[d][21], Цитоскелет[d][2], нуклеоплазма[d][2], Центр организации микротрубочек[d][2], nuclear chromosome[d][22], Митохондриальный матрикс[d][2], ядрышко[d][2], митохондрия[d][2][23], perinuclear region of cytoplasm[d][2][24], хроматин[d][19], Төш[2][2][15][…], цитозоль[d][2], protein-containing complex[d][8], condensed chromosome[d][2], condensed nuclear chromosome[d][3], lateral element[d][25], condensed nuclear chromosome[d][2][4] һәм Хромосома[2]
Биологический процесс strand invasion[d][4], mitotic recombination-dependent replication fork processing[d][2], reciprocal meiotic recombination[d][26], DNA recombination[d][16][2], regulation of double-strand break repair via homologous recombination[d][22], процесс метаболизма ДНК[d][2], positive regulation of DNA ligation[d][17], cellular response to camptothecin[d][27], double-strand break repair via homologous recombination[d][28][15][27][…], cellular response to ionizing radiation[d][22][27], mitotic recombination[d][26], protein homooligomerization[d][11], репарация ДНК[d][29][2][2], DNA unwinding involved in DNA replication[d][16], cellular response to DNA damage stimulus[d][15][2][27][…], interstrand cross-link repair[d][30], DNA recombinase assembly[d][13], negative regulation of G0 to G1 transition[d][2], telomere maintenance via recombination[d][31], telomere maintenance via telomere lengthening[d][31], replication fork processing[d][32][19], мейоз[d][2], chromosome organization involved in meiotic cell cycle[d][4], DNA recombinase assembly[d][15][4], mitotic recombination[d][29][4] һәм reciprocal meiotic recombination[d][29][4]
Изображение Gene Atlas

RAD51 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[33][34]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. 1,0 1,1 UniProt
  2. 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 UniProt-GOA
  3. 3,0 3,1 3,2 3,3 3,4 3,5 UniProt-GOA
  4. 4,0 4,1 4,2 4,3 4,4 4,5 4,6 4,7 Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform.OUP, 2011. — ISSN 1467-5463; 1477-4054doi:10.1093/BIB/BBR042PMID:21873635
  5. Moldovan G., Madhavan M. V., Mirchandani K. D. et al. DNA polymerase POLN participates in cross-link repair and homologous recombination // Mol. Cell. Biol.ASM, 2010. — ISSN 0270-7306; 1098-5549; 1067-8824doi:10.1128/MCB.01124-09PMID:19995904
  6. Davies O. R. Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats // Nat. Struct. Mol. Biol.USA: NPG, 2007. — ISSN 1545-9993; 1545-9985doi:10.1038/NSMB1251PMID:17515903
  7. Yuan Z. M., Y Huang, T Ishiko et al. Regulation of Rad51 function by c-Abl in response to DNA damage // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1998. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.273.7.3799PMID:9461559
  8. 8,0 8,1 Kovalenko O. V., Wiese C., Schild D. RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51. // Nucleic Acids Res.OUP, University of Oxford, 2006. — ISSN 0305-1048; 1362-4962; 1362-4954doi:10.1093/NAR/GKL665PMID:16990250
  9. 9,0 9,1 Kovalenko O. V., Golub E. I., P Bray-Ward et al. A novel nucleic acid-binding protein that interacts with human rad51 recombinase // Nucleic Acids Res.OUP, University of Oxford, 1997. — ISSN 0305-1048; 1362-4962; 1362-4954doi:10.1093/NAR/25.24.4946PMID:9396801
  10. Dosanjh M. K., Collins D. W., W Fan et al. Isolation and characterization of RAD51C, a new human member of the RAD51 family of related genes // Nucleic Acids Res.OUP, University of Oxford, 1998. — ISSN 0305-1048; 1362-4962; 1362-4954doi:10.1093/NAR/26.5.1179PMID:9469824
  11. 11,0 11,1 Blundell T. L. Insights into DNA recombination from the structure of a RAD51-BRCA2 complex // Nature / M. SkipperNPG, Springer Science+Business Media, 2002. — ISSN 1476-4687; 0028-0836doi:10.1038/NATURE01230PMID:12442171
  12. Benthem J. v., Wesoly J., Galjart N. Differential contributions of mammalian Rad54 paralogs to recombination, DNA damage repair, and meiosis // Mol. Cell. Biol.ASM, 2006. — ISSN 0270-7306; 1098-5549; 1067-8824doi:10.1128/MCB.26.3.976-989.2006PMID:16428451
  13. 13,0 13,1 13,2 Joenje H., Meijers-Heijboer H., Dunnen J. d. et al. A novel Fanconi anaemia subtype associated with a dominant-negative mutation in RAD51 // Nat. Commun. / J. HeberNPG, 2015. — ISSN 2041-1723doi:10.1038/NCOMMS9829PMID:26681308
  14. 14,0 14,1 Benson F. E., West S. C. Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA // EMBO J.NPG, 1994. — ISSN 0261-4189; 1460-2075doi:10.1002/J.1460-2075.1994.TB06914.XPMID:7988572
  15. 15,0 15,1 15,2 15,3 15,4 15,5 15,6 15,7 Joenje H., Meijers-Heijboer H., Dunnen J. d. et al. A novel Fanconi anaemia subtype associated with a dominant-negative mutation in RAD51 // Nat. Commun. / J. HeberNPG, 2015. — ISSN 2041-1723doi:10.1038/NCOMMS9829PMID:26681308
  16. 16,0 16,1 16,2 16,3 16,4 Benson F. E., West S. C. Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA // EMBO J.NPG, 1994. — ISSN 0261-4189; 1460-2075doi:10.1002/J.1460-2075.1994.TB06914.XPMID:7988572
  17. 17,0 17,1 Baumann P., Benson F. E., West S. C. Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro // CellCell Press, Elsevier BV, 1996. — ISSN 0092-8674; 1097-4172doi:10.1016/S0092-8674(00)81394-XPMID:8929543
  18. 18,0 18,1 Long D. T., Gambus A., Dutta A. et al. The MCM8-MCM9 complex promotes RAD51 recruitment at DNA damage sites to facilitate homologous recombination // Mol. Cell. Biol.ASM, 2013. — ISSN 0270-7306; 1098-5549; 1067-8824doi:10.1128/MCB.01503-12PMID:23401855
  19. 19,0 19,1 19,2 Beli P., Hanada K. FBH1 influences DNA replication fork stability and homologous recombination through ubiquitylation of RAD51 // Nat. Commun. / J. HeberNPG, 2015. — ISSN 2041-1723doi:10.1038/NCOMMS6931PMID:25585578
  20. Huggins D. J., Jeyasekharan A. PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2014. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.1317585111PMID:24550317
  21. O Bischof, Kim S. H., J Irving et al. Regulation and localization of the Bloom syndrome protein in response to DNA damage // J. Cell Biol. / J. NunnariRockefeller University Press, 2001. — ISSN 0021-9525; 1540-8140doi:10.1083/JCB.153.2.367PMID:11309417
  22. 22,0 22,1 22,2 Yuan J., Chen J. FIGNL1-containing protein complex is required for efficient homologous recombination repair // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2013. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.1220662110PMID:23754376
  23. Sage J. M., Gildemeister O. S., Knight K. L. Discovery of a novel function for human Rad51: maintenance of the mitochondrial genome // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2010. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M109.099846PMID:20413593
  24. Bennett B. T., Knight K. L. Cellular localization of human Rad51C and regulation of ubiquitin-mediated proteolysis of Rad51 // J. Cell. Biochem.Wiley, 2005. — ISSN 0730-2312; 1097-4644; 0733-1959doi:10.1002/JCB.20640PMID:16215984
  25. Couch F. J. Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells // Mol. CellCell Press, Elsevier BV, 1998. — ISSN 1097-2765; 1097-4164doi:10.1016/S1097-2765(00)80276-2PMID:9774970
  26. 26,0 26,1 A Shinohara, H Ogawa, Y Matsuda et al. Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA // Nature Genetics / M. Axton, T. FaialNPG, 1993. — ISSN 1061-4036; 1546-1718doi:10.1038/NG0793-239PMID:8358431
  27. 27,0 27,1 27,2 27,3 Wan L., Han J., Liu T. et al. Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2013. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.1220921110PMID:23509288
  28. Lio Y., Mazin A. V., Kowalczykowski S. C. et al. Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2003. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M211038200PMID:12427746
  29. 29,0 29,1 29,2 A Shinohara, H Ogawa, Y Matsuda et al. Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA // Nature Genetics / M. Axton, T. FaialNPG, 1993. — ISSN 1061-4036; 1546-1718doi:10.1038/NG0793-239PMID:8358431
  30. Smogorzewska A., Wang A. T., Zierhut H. et al. A Dominant Mutation in Human RAD51 Reveals Its Function in DNA Interstrand Crosslink Repair Independent of Homologous Recombination // Mol. CellCell Press, Elsevier BV, 2015. — ISSN 1097-2765; 1097-4164doi:10.1016/J.MOLCEL.2015.07.009PMID:26253028
  31. 31,0 31,1 Carlos A. R., Blasco M. A., Benitez J. BRCA2 acts as a RAD51 loader to facilitate telomere replication and capping // Nat. Struct. Mol. Biol.USA: NPG, 2010. — ISSN 1545-9993; 1545-9985doi:10.1038/NSMB.1943PMID:21076401
  32. Kim T. M., Ko J. H., Hu L. et al. RAD51 mutants cause replication defects and chromosomal instability // Mol. Cell. Biol.ASM, 2012. — ISSN 0270-7306; 1098-5549; 1067-8824doi:10.1128/MCB.00406-12PMID:22778135
  33. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). 18 сентябрь, 2017 тикшерелгән.
  34. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар[үзгәртү | вики-текстны үзгәртү]

  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)