MRE11A
From Wikipedia, the free encyclopedia
Double-strand break repair protein MRE11A is a protein that in humans is encoded by the MRE11A gene.[1]
Function
This gene encodes a nuclear protein involved in homologous recombination, telomere length maintenance, and DNA double-strand break repair. By itself, the protein has 3' to 5' exonuclease activity and endonuclease activity. The protein forms a complex with the RAD50 homolog; this complex is required for nonhomologous joining of DNA ends and possesses increased single-stranded DNA endonuclease and 3' to 5' exonuclease activities. In conjunction with a DNA ligase, this protein promotes the joining of noncomplementary ends in vitro using short homologies near the ends of the DNA fragments. This gene has a pseudogene on chromosome 3. Alternative splicing of this gene results in two transcript variants encoding different isoforms.[2]
Orthologs of MRE11A
Mre11, an ortholog of human MRE11A, occurs in the prokaryote archaeon Sulfolobus acidocaldarius.[3] In this organism the Mre11 protein interacts with the Rad50 protein and appears to have an active role in the repair of DNA damages experimentally introduced by gamma radiation.[3] Similarly, during meiosis in the eukaryotic protist Tetrahymena Mre11 is required for repair of DNA damages, in this case double-strand breaks,[4] by a process that likely involves homologous recombination. These observations suggest that human MRE11A is descended from prokaryotic and protist ancestral Mre11 proteins that served a role in early processes for repairing DNA damage.
Interactions
MRE11A has been shown to interact with:
- ATM,[5][6]
- BRCA1,[6][7][8][9]
- Ku70,[10]
- MDC1,[11]
- NBN,[6][12][13][14][15]
- Rad50,[6][7][10][12][16] and
- TERF2.[17]
See also
References
- ↑ Petrini JH, Walsh ME, DiMare C, Chen XN, Korenberg JR, Weaver DT (February 1996). "Isolation and characterization of the human MRE11 homologue". Genomics 29 (1): 80–6. doi:10.1006/geno.1995.1217. PMID 8530104.
- ↑ "Entrez Gene: MRE11A MRE11 meiotic recombination 11 homolog A (S. cerevisiae)".
- ↑ 3.0 3.1 Quaiser A, Constantinesco F, White MF, Forterre P, Elie C (2008). "The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldarius". BMC Mol. Biol. 9: 25. doi:10.1186/1471-2199-9-25. PMC 2288612. PMID 18294364.
- ↑ Lukaszewicz A, Howard-Till RA, Novatchkova M, Mochizuki K, Loidl J (October 2010). "MRE11 and COM1/SAE2 are required for double-strand break repair and efficient chromosome pairing during meiosis of the protist Tetrahymena". Chromosoma 119 (5): 505–18. doi:10.1007/s00412-010-0274-9. PMID 20422424.
- ↑ Kim ST, Lim DS, Canman CE, Kastan MB (1999). "Substrate specificities and identification of putative substrates of ATM kinase family members". J. Biol. Chem. 274 (53): 37538–43. doi:10.1074/jbc.274.53.37538. PMID 10608806.
- ↑ 6.0 6.1 6.2 6.3 Wang Y, Cortez D, Yazdi P, Neff N, Elledge SJ, Qin J (2000). "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures". Genes Dev. 14 (8): 927–39. PMC 316544. PMID 10783165.
- ↑ 7.0 7.1 Chiba N, Parvin JD (2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". J. Biol. Chem. 276 (42): 38549–54. doi:10.1074/jbc.M105227200. PMID 11504724.
- ↑ Paull TT, Cortez D, Bowers B, Elledge SJ, Gellert M (2001). "Direct DNA binding by Brca1". Proc. Natl. Acad. Sci. U.S.A. 98 (11): 6086–91. doi:10.1073/pnas.111125998. PMC 33426. PMID 11353843.
- ↑ Zhong Q, Chen CF, Li S, Chen Y, Wang CC, Xiao J, Chen PL, Sharp ZD, Lee WH (1999). "Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response". Science 285 (5428): 747–50. doi:10.1126/science.285.5428.747. PMID 10426999.
- ↑ 10.0 10.1 Goedecke W, Eijpe M, Offenberg HH, van Aalderen M, Heyting C (1999). "Mre11 and Ku70 interact in somatic cells, but are differentially expressed in early meiosis". Nat. Genet. 23 (2): 194–8. doi:10.1038/13821. PMID 10508516.
- ↑ Xu X, Stern DF (2003). "NFBD1/MDC1 regulates ionizing radiation-induced focus formation by DNA checkpoint signaling and repair factors". FASEB J. 17 (13): 1842–8. doi:10.1096/fj.03-0310com. PMID 14519663.
- ↑ 12.0 12.1 Trujillo KM, Yuan SS, Lee EY, Sung P (1998). "Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95". J. Biol. Chem. 273 (34): 21447–50. doi:10.1074/jbc.273.34.21447. PMID 9705271.
- ↑ Cerosaletti KM, Concannon P (2003). "Nibrin forkhead-associated domain and breast cancer C-terminal domain are both required for nuclear focus formation and phosphorylation". J. Biol. Chem. 278 (24): 21944–51. doi:10.1074/jbc.M211689200. PMID 12679336.
- ↑ Matsuzaki K, Shinohara A, Shinohara M (2008). "Forkhead-associated domain of yeast Xrs2, a homolog of human Nbs1, promotes nonhomologous end joining through interaction with a ligase IV partner protein, Lif1". Genetics 179 (1): 213–25. doi:10.1534/genetics.107.079236. PMC 2390601. PMID 18458108.
- ↑ Desai-Mehta A, Cerosaletti KM, Concannon P (2001). "Distinct functional domains of nibrin mediate Mre11 binding, focus formation, and nuclear localization". Mol. Cell. Biol. 21 (6): 2184–91. doi:10.1128/MCB.21.6.2184-2191.2001. PMC 86852. PMID 11238951.
- ↑ Dolganov GM, Maser RS, Novikov A, Tosto L, Chong S, Bressan DA, Petrini JH (1996). "Human Rad50 is physically associated with human Mre11: identification of a conserved multiprotein complex implicated in recombinational DNA repair". Mol. Cell. Biol. 16 (9): 4832–41. PMC 231485. PMID 8756642.
- ↑ Zhu XD, Küster B, Mann M, Petrini JH, de Lange T (2000). "Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres". Nat. Genet. 25 (3): 347–52. doi:10.1038/77139. PMID 10888888.
Further reading
- Dolganov GM, Maser RS, Novikov A, et al. (1996). "Human Rad50 is physically associated with human Mre11: identification of a conserved multiprotein complex implicated in recombinational DNA repair.". Mol. Cell. Biol. 16 (9): 4832–41. PMC 231485. PMID 8756642.
- Carney JP, Maser RS, Olivares H, et al. (1998). "The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response.". Cell 93 (3): 477–86. doi:10.1016/S0092-8674(00)81175-7. PMID 9590181.
- Paull TT, Gellert M (1998). "The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks.". Mol. Cell 1 (7): 969–79. doi:10.1016/S1097-2765(00)80097-0. PMID 9651580.
- Trujillo KM, Yuan SS, Lee EY, Sung P (1998). "Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95.". J. Biol. Chem. 273 (34): 21447–50. doi:10.1074/jbc.273.34.21447. PMID 9705271.
- Chamankhah M, Wei YF, Xiao W (1999). "Isolation of hMRE11B: failure to complement yeast mre11 defects due to species-specific protein interactions.". Gene 225 (1-2): 107–16. doi:10.1016/S0378-1119(98)00530-7. PMID 9931460.
- Zhong Q, Chen CF, Li S, et al. (1999). "Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response.". Science 285 (5428): 747–50. doi:10.1126/science.285.5428.747. PMID 10426999.
- Goedecke W, Eijpe M, Offenberg HH, et al. (1999). "Mre11 and Ku70 interact in somatic cells, but are differentially expressed in early meiosis.". Nat. Genet. 23 (2): 194–8. doi:10.1038/13821. PMID 10508516.
- Kim ST, Lim DS, Canman CE, Kastan MB (2000). "Substrate specificities and identification of putative substrates of ATM kinase family members.". J. Biol. Chem. 274 (53): 37538–43. doi:10.1074/jbc.274.53.37538. PMID 10608806.
- Stewart GS, Maser RS, Stankovic T, et al. (2000). "The DNA double-strand break repair gene hMRE11 is mutated in individuals with an ataxia-telangiectasia-like disorder.". Cell 99 (6): 577–87. doi:10.1016/S0092-8674(00)81547-0. PMID 10612394.
- Wang Y, Cortez D, Yazdi P, et al. (2000). "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures.". Genes Dev. 14 (8): 927–39. PMC 316544. PMID 10783165.
- Gatei M, Young D, Cerosaletti KM, et al. (2000). "ATM-dependent phosphorylation of nibrin in response to radiation exposure.". Nat. Genet. 25 (1): 115–9. doi:10.1038/75508. PMID 10802669.
- Zhu XD, Küster B, Mann M, et al. (2000). "Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres.". Nat. Genet. 25 (3): 347–52. doi:10.1038/77139. PMID 10888888.
- de Vries H, Rüegsegger U, Hübner W, et al. (2000). "Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors.". EMBO J. 19 (21): 5895–904. doi:10.1093/emboj/19.21.5895. PMC 305781. PMID 11060040.
- Fukuda T, Sumiyoshi T, Takahashi M, et al. (2001). "Alterations of the double-strand break repair gene MRE11 in cancer.". Cancer Res. 61 (1): 23–6. PMID 11196167.
- Desai-Mehta A, Cerosaletti KM, Concannon P (2001). "Distinct functional domains of nibrin mediate Mre11 binding, focus formation, and nuclear localization.". Mol. Cell. Biol. 21 (6): 2184–91. doi:10.1128/MCB.21.6.2184-2191.2001. PMC 86852. PMID 11238951.
- Paull TT, Cortez D, Bowers B, et al. (2001). "Direct DNA binding by Brca1.". Proc. Natl. Acad. Sci. U.S.A. 98 (11): 6086–91. doi:10.1073/pnas.111125998. PMC 33426. PMID 11353843.
- Hopfner KP, Karcher A, Craig L, et al. (2001). "Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase.". Cell 105 (4): 473–85. doi:10.1016/S0092-8674(01)00335-X. PMID 11371344.
- Pitts SA, Kullar HS, Stankovic T, et al. (2001). "hMRE11: genomic structure and a null mutation identified in a transcript protected from nonsense-mediated mRNA decay.". Hum. Mol. Genet. 10 (11): 1155–62. doi:10.1093/hmg/10.11.1155. PMID 11371508.
- Chiba N, Parvin JD (2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage.". J. Biol. Chem. 276 (42): 38549–54. doi:10.1074/jbc.M105227200. PMID 11504724.
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