메뉴 건너뛰기




Volumn 35, Issue 17, 2015, Pages 2910-2917

A single conserved residue mediates binding of the ribonucleotide reductase catalytic subunit RRM1 to RRM2 and is essential for mouse development

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEOTIDE REDUCTASE; RRM1 PROTEIN; RRM2 PROTEIN; UNCLASSIFIED DRUG; H2AX PROTEIN, MOUSE; HISTONE; MUCIN; MUSCLE PROTEIN; PEPTIDE; PROTEIN BINDING; RIBONUCLEOSIDE DIPHOSPHATE REDUCTASE; RIBONUCLEOTIDE REDUCTASE M2; RRM1 PROTEIN, MOUSE; TFF2 PROTEIN, MOUSE;

EID: 84938853170     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00475-15     Document Type: Article
Times cited : (9)

References (27)
  • 1
    • 84919361106 scopus 로고    scopus 로고
    • Replication stress and cancer: it takes two to tango
    • Lecona E, Fernandez-Capetillo O. 2014. Replication stress and cancer: it takes two to tango. Exp Cell Res 329:26-34. http://dx.doi.org/10.1016/j.yexcr.2014.09.019.
    • (2014) Exp Cell Res , vol.329 , pp. 26-34
    • Lecona, E.1    Fernandez-Capetillo, O.2
  • 3
    • 78649443528 scopus 로고    scopus 로고
    • The ATR barrier to replication-born DNA damage
    • Lopez-Contreras AJ, Fernandez-Capetillo O. 2010. The ATR barrier to replication-born DNA damage. DNA Repair (Amst) 9:1249-1255. http://dx.doi.org/10.1016/j.dnarep.2010.09.012.
    • (2010) DNA Repair (Amst) , vol.9 , pp. 1249-1255
    • Lopez-Contreras, A.J.1    Fernandez-Capetillo, O.2
  • 4
    • 47749141560 scopus 로고    scopus 로고
    • ATR: an essential regulator of genome integrity
    • Cimprich KA, Cortez D. 2008. ATR: an essential regulator of genome integrity. Nat Rev Mol Cell Biol 9:616-627. http://dx.doi.org/10.1038/nrm2450.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 616-627
    • Cimprich, K.A.1    Cortez, D.2
  • 5
    • 0032483576 scopus 로고    scopus 로고
    • The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor
    • Huang M, Zhou Z, Elledge SJ. 1998. The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor. Cell 94:595-605. http://dx.doi.org/10.1016/S0092-8674(00)81601-3.
    • (1998) Cell , vol.94 , pp. 595-605
    • Huang, M.1    Zhou, Z.2    Elledge, S.J.3
  • 6
    • 0032161269 scopus 로고    scopus 로고
    • A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools
    • Zhao X, Muller EG, Rothstein R. 1998. A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools. Mol Cell 2:329-340. http://dx.doi.org/10.1016/S1097-2765(00)80277-4.
    • (1998) Mol Cell , vol.2 , pp. 329-340
    • Zhao, X.1    Muller, E.G.2    Rothstein, R.3
  • 8
    • 33746370368 scopus 로고    scopus 로고
    • Ribonucleotide reductases
    • Nordlund P, Reichard P. 2006. Ribonucleotide reductases. Annu Rev Biochem 75:681-706. http://dx.doi.org/10.1146/annurev.biochem.75.103004.142443.
    • (2006) Annu Rev Biochem , vol.75 , pp. 681-706
    • Nordlund, P.1    Reichard, P.2
  • 9
    • 33847779064 scopus 로고    scopus 로고
    • Role of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1
    • Zhang Z, Yang K, Chen CC, Feser J, Huang M. 2007. Role of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1. Proc Natl Acad Sci U S A 104:2217-2222. http://dx.doi.org/10.1073/pnas.0611095104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2217-2222
    • Zhang, Z.1    Yang, K.2    Chen, C.C.3    Feser, J.4    Huang, M.5
  • 10
    • 0037423223 scopus 로고    scopus 로고
    • Survival of DNA damage in yeast directly depends on increased dNTP levels allowed by relaxed feedback inhibition of ribonucleotide reductase
    • Chabes A, Georgieva B, Domkin V, Zhao X, Rothstein R, Thelander L. 2003. Survival of DNA damage in yeast directly depends on increased dNTP levels allowed by relaxed feedback inhibition of ribonucleotide reductase. Cell 112:391-401. http://dx.doi.org/10.1016/S0092-8674(03)00075-8.
    • (2003) Cell , vol.112 , pp. 391-401
    • Chabes, A.1    Georgieva, B.2    Domkin, V.3    Zhao, X.4    Rothstein, R.5    Thelander, L.6
  • 12
    • 0019522434 scopus 로고
    • Mutator phenotypes in mammalian cell mutants with distinct biochemical defects and abnormal deoxyribonucleoside triphosphate pools
    • Weinberg G, Ullman B, Martin DW, Jr. 1981. Mutator phenotypes in mammalian cell mutants with distinct biochemical defects and abnormal deoxyribonucleoside triphosphate pools. Proc Natl Acad Sci U S A 78:2447-2451. http://dx.doi.org/10.1073/pnas.78.4.2447.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 2447-2451
    • Weinberg, G.1    Ullman, B.2    Martin, D.W.3
  • 13
    • 33746539166 scopus 로고    scopus 로고
    • DNA precursor metabolism and genomic stability
    • Mathews CK. 2006. DNA precursor metabolism and genomic stability. FASEB J 20:1300-1314. http://dx.doi.org/10.1096/fj.06-5730rev.
    • (2006) FASEB J , vol.20 , pp. 1300-1314
    • Mathews, C.K.1
  • 14
    • 0034594978 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage
    • Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y. 2000. A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature 404:42-49. http://dx.doi.org/10.1038/35003506.
    • (2000) Nature , vol.404 , pp. 42-49
    • Tanaka, H.1    Arakawa, H.2    Yamaguchi, T.3    Shiraishi, K.4    Fukuda, S.5    Matsui, K.6    Takei, Y.7    Nakamura, Y.8
  • 15
    • 0034738967 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene is a transcriptional target of p53 and p73
    • Nakano K, Balint E, Ashcroft M, Vousden KH. 2000. A ribonucleotide reductase gene is a transcriptional target of p53 and p73. Oncogene 19:4283-4289. http://dx.doi.org/10.1038/sj.onc.1203774.
    • (2000) Oncogene , vol.19 , pp. 4283-4289
    • Nakano, K.1    Balint, E.2    Ashcroft, M.3    Vousden, K.H.4
  • 17
    • 0033579443 scopus 로고    scopus 로고
    • Yeast Sml1, a protein inhibitor of ribonucleotide reductase
    • Chabes A, Domkin V, Thelander L. 1999. Yeast Sml1, a protein inhibitor of ribonucleotide reductase. J Biol Chem 274:36679-36683. http://dx.doi.org/10.1074/jbc.274.51.36679.
    • (1999) J Biol Chem , vol.274 , pp. 36679-36683
    • Chabes, A.1    Domkin, V.2    Thelander, L.3
  • 18
    • 0035796505 scopus 로고    scopus 로고
    • The ribonucleotide reductase inhibitor Sml1 is a new target of the Mec1/Rad53 kinase cascade during growth and in response to DNA damage
    • Zhao X, Chabes A, Domkin V, Thelander L, Rothstein R. 2001. The ribonucleotide reductase inhibitor Sml1 is a new target of the Mec1/Rad53 kinase cascade during growth and in response to DNA damage. EMBO J 20:3544-3553. http://dx.doi.org/10.1093/emboj/20.13.3544.
    • (2001) EMBO J , vol.20 , pp. 3544-3553
    • Zhao, X.1    Chabes, A.2    Domkin, V.3    Thelander, L.4    Rothstein, R.5
  • 19
    • 84907192516 scopus 로고    scopus 로고
    • Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes
    • Arnaoutov A, Dasso M. 2014. Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes. Science 345:1512-1515. http://dx.doi.org/10.1126/science.1251550.
    • (2014) Science , vol.345 , pp. 1512-1515
    • Arnaoutov, A.1    Dasso, M.2
  • 20
    • 78049369559 scopus 로고    scopus 로고
    • The ribonucleotide reductase inhibitor, Sml1, is sequentially phosphorylated, ubiquitylated and degraded in response to DNA damage
    • Andreson BL, Gupta A, Georgieva BP, Rothstein R. 2010. The ribonucleotide reductase inhibitor, Sml1, is sequentially phosphorylated, ubiquitylated and degraded in response to DNA damage. Nucleic Acids Res 38:6490-6501. http://dx.doi.org/10.1093/nar/gkq552.
    • (2010) Nucleic Acids Res , vol.38 , pp. 6490-6501
    • Andreson, B.L.1    Gupta, A.2    Georgieva, B.P.3    Rothstein, R.4
  • 21
    • 47949131755 scopus 로고    scopus 로고
    • Upregulation of annexin A1 expression by butyrate in human colon adenocarcinoma cells: role of p53, NF-Y, and p38 mitogen-activated protein kinase
    • Lecona E, Barrasa JI, Olmo N, Llorente B, Turnay J, Lizarbe MA. 2008. Upregulation of annexin A1 expression by butyrate in human colon adenocarcinoma cells: role of p53, NF-Y, and p38 mitogen-activated protein kinase. Mol Cell Biol 28:4665-4674. http://dx.doi.org/10.1128/MCB.00650-07.
    • (2008) Mol Cell Biol , vol.28 , pp. 4665-4674
    • Lecona, E.1    Barrasa, J.I.2    Olmo, N.3    Llorente, B.4    Turnay, J.5    Lizarbe, M.A.6
  • 26
    • 84910621526 scopus 로고    scopus 로고
    • functional approach reveals a genetic and physical interaction between ribonucleotide reductase and CHK1 in mammalian cells
    • Taricani L, Shanahan F, Malinao MC, Beaumont M, Parry DA. 2014. functional approach reveals a genetic and physical interaction between ribonucleotide reductase and CHK1 in mammalian cells. PLoS One 9:e111714. http://dx.doi.org/10.1371/journal.pone.0111714.
    • (2014) PLoS One , vol.9
    • Taricani, L.1    Shanahan, F.2    Malinao, M.C.3    Beaumont, M.4    Parry, D.A.5
  • 27
    • 84875923444 scopus 로고    scopus 로고
    • ERCC1 and RRM1: ready for prime time?
    • Besse B, Olaussen KA, Soria JC. 2013. ERCC1 and RRM1: ready for prime time? J Clin Oncol 31:1050-1060. http://dx.doi.org/10.1200/JCO.2012.43.0900.
    • (2013) J Clin Oncol , vol.31 , pp. 1050-1060
    • Besse, B.1    Olaussen, K.A.2    Soria, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.