메뉴 건너뛰기




Volumn 24, Issue 11, 2010, Pages 1145-1159

Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms

Author keywords

Cullin 4; Intrinsically disordered proteins; Nuclear import; Ribonucleotide reductase

Indexed keywords

DIF1 PROTEIN; FUNGAL PROTEIN; RIBONUCLEOTIDE REDUCTASE; SACCHAROMYCES CEREVISIAE PROTEIN; SPD1 PROTEIN; UNCLASSIFIED DRUG;

EID: 77953072305     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.561910     Document Type: Article
Times cited : (39)

References (35)
  • 1
    • 0032826786 scopus 로고    scopus 로고
    • NORF5/HUG1 is a component of the MEC1-mediated checkpoint response to DNA damage and replication arrest in Saccharomyces cerevisiae
    • Basrai MA, Velculescu VE, Kinzler KW, Hieter P. 1999. NORF5/HUG1 is a component of the MEC1-mediated checkpoint response to DNA damage and replication arrest in Saccharomyces cerevisiae. Mol Cell Biol 19: 7041-7049. (Pubitemid 29441886)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.10 , pp. 7041-7049
    • Basrai, M.A.1    Velculescu, V.E.2    Kinzler, K.W.3    Hieter, P.4
  • 2
    • 33845627767 scopus 로고    scopus 로고
    • Analyzing the dose-dependence of the Saccharomyces cerevisiae global transcriptional response to methyl methane-sulfonate and ionizing radiation
    • doi: 10.1186/1471-2164-7-305
    • Benton MG, Somasundaram S, Glasner JD, Palecek SP. 2006. Analyzing the dose-dependence of the Saccharomyces cerevisiae global transcriptional response to methyl methane-sulfonate and ionizing radiation. BMC Genomics 7: 305. doi: 10.1186/1471-2164-7-305.
    • (2006) BMC Genomics , vol.7 , pp. 305
    • Benton, M.G.1    Somasundaram, S.2    Glasner, J.D.3    Palecek, S.P.4
  • 3
    • 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.
    • (1999) J Biol Chem , vol.274 , pp. 36679-36683
    • Chabes, A.1    Domkin, V.2    Thelander, L.3
  • 4
    • 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
    • DOI 10.1016/S0092-8674(03)00075-8
    • 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. (Pubitemid 36183658)
    • (2003) Cell , vol.112 , Issue.3 , pp. 391-401
    • Chabes, A.1    Georgieva, B.2    Domkin, V.3    Zhao, X.4    Rothstein, R.5    Thelander, L.6
  • 5
    • 0022455333 scopus 로고
    • Specific inhibition of herpesvirus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit 2
    • Cohen EA, Gaudreau P, Brazeau P, Langelier Y. 1986. Specific inhibition of herpesvirus ribonucleotide reductase by a non-apeptide derived from the carboxy terminus of subunit 2. Nature 321: 441-443. (Pubitemid 16055498)
    • (1986) Nature , vol.321 , Issue.6068 , pp. 441-443
    • Cohen, E.A.1    Gaudreau, P.2    Brazeau, P.3    Langelier, Y.4
  • 7
    • 33747017731 scopus 로고    scopus 로고
    • Constraining G1-Specific Transcription to Late G1 Phase: The MBF-Associated Corepressor Nrm1 Acts via Negative Feedback
    • DOI 10.1016/j.molcel.2006.06.025, PII S1097276506004539
    • de Bruin RA, Kalashnikova TI, Chahwan C, McDonald WH, Wohlschlegel J, Yates J 3rd, Russell P, Wittenberg C. 2006. Constraining G1-specific transcription to late G1 phase: The MBF-associated corepressor Nrm1 acts via negative feedback. Mol Cell 23: 483-496. (Pubitemid 44205489)
    • (2006) Molecular Cell , vol.23 , Issue.4 , pp. 483-496
    • De Bruin, R.A.M.1    Kalashnikova, T.I.2    Chahwan, C.3    McDonald, W.H.4    Wohlschlegel, J.5    Yates III, J.6    Russell, P.7    Wittenberg, C.8
  • 9
    • 0027605113 scopus 로고
    • DNA damage and cell cycle regulation of ribonucleotide reductase
    • Elledge SJ, Zhou Z, Allen JB, Navas TA. 1993. DNA damage and cell cycle regulation of ribonucleotide reductase. Bioessays 15: 333-339.
    • (1993) Bioessays , vol.15 , pp. 333-339
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3    Navas, T.A.4
  • 11
    • 0027333305 scopus 로고
    • P63cdc13, a B-type cyclin, is associated with both the nucleolar and chromatin domains of the fission yeast nucleus
    • Gallagher IM, Alfa CE, Hyams JS. 1993. p63cdc13, a B-type cyclin, is associated with both the nucleolar and chromatin domains of the fission yeast nucleus. Mol Biol Cell 4: 1087-1096.
    • (1993) Mol Biol Cell , vol.4 , pp. 1087-1096
    • Gallagher, I.M.1    Alfa, C.E.2    Hyams, J.S.3
  • 12
    • 33644972445 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe replication inhibitor Spd1 regulates ribonucleotide reductase activity and dNTPs by binding to the large Cdc22 subunit
    • Hakansson P, Dahl L, Chilkova O, Domkin V, Thelander L. 2006. The Schizosaccharomyces pombe replication inhibitor Spd1 regulates ribonucleotide reductase activity and dNTPs by binding to the large Cdc22 subunit. J Biol Chem 281: 1778-1783.
    • (2006) J Biol Chem , vol.281 , pp. 1778-1783
    • Hakansson, P.1    Dahl, L.2    Chilkova, O.3    Domkin, V.4    Thelander, L.5
  • 14
    • 34547588389 scopus 로고    scopus 로고
    • PrDOS: Prediction of disordered protein regions from amino acid sequence
    • doi: 10.1093/nar/gkm363
    • Ishida T, Kinoshita K. 2007. PrDOS: Prediction of disordered protein regions from amino acid sequence. Nucleic Acids Res 35: W460-W464. doi: 10.1093/nar/gkm363.
    • (2007) Nucleic Acids Res , vol.35
    • Ishida, T.1    Kinoshita, K.2
  • 15
    • 32044442056 scopus 로고    scopus 로고
    • Control of ribonucleotide reductase localization through an anchoring mechanism involving Wtm1
    • Lee YD, Elledge SJ. 2006. Control of ribonucleotide reductase localization through an anchoring mechanism involving Wtm1. Genes Dev 20: 334-344.
    • (2006) Genes Dev , vol.20 , pp. 334-344
    • Lee, Y.D.1    Elledge, S.J.2
  • 16
    • 53349151829 scopus 로고    scopus 로고
    • Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase
    • Lee YD, Wang J, Stubbe J, Elledge SJ. 2008. Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase. Mol Cell 32: 70-80.
    • (2008) Mol Cell , vol.32 , pp. 70-80
    • Lee, Y.D.1    Wang, J.2    Stubbe, J.3    Elledge, S.J.4
  • 17
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms
    • Liu C, Powell KA, Mundt K, Wu L, Carr AM, Caspari T. 2003. Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms. Genes Dev 17: 1130-1140.
    • (2003) Genes Dev , vol.17 , pp. 1130-1140
    • Liu, C.1    Powell, K.A.2    Mundt, K.3    Wu, L.4    Carr, A.M.5    Caspari, T.6
  • 20
    • 0037082119 scopus 로고    scopus 로고
    • Ribonucleotide reductases: The evolution of allosteric regulation
    • Reichard P. 2002. Ribonucleotide reductases: The evolution of allosteric regulation. Arch Biochem Biophys 397: 149-155.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 149-155
    • Reichard, P.1
  • 21
    • 33748785426 scopus 로고    scopus 로고
    • Enzymatically active mammalian ribonucleotide reductase exists primarily as an a6b2 octamer
    • Rofougaran R, Vodnala M, Hofer A. 2006. Enzymatically active mammalian ribonucleotide reductase exists primarily as an a6b2 octamer. J Biol Chem 281: 27705-27711.
    • (2006) J Biol Chem , vol.281 , pp. 27705-27711
    • Rofougaran, R.1    Vodnala, M.2    Hofer, A.3
  • 22
    • 58149091633 scopus 로고    scopus 로고
    • Oligomerization status directs overall activity regulation of the Escherichia coli class Ia ribonucleotide reductase
    • Rofougaran R, Crona M, Vodnala M, Sjoberg BM, Hofer A. 2008. Oligomerization status directs overall activity regulation of the Escherichia coli class Ia ribonucleotide reductase. J Biol Chem 283: 35310-35318.
    • (2008) J Biol Chem , vol.283 , pp. 35310-35318
    • Rofougaran, R.1    Crona, M.2    Vodnala, M.3    Sjoberg, B.M.4    Hofer, A.5
  • 23
    • 0345552249 scopus 로고    scopus 로고
    • Simultaneous determination of pyrimidine or purine deoxyribonucleoside triphosphates using a polymerase assay
    • Roy B, Beuneu C, Roux P, Buc H, Lemaire G, Lepoivre M. 1999. Simultaneous determination of pyrimidine or purine deoxyribonucleoside triphosphates using a polymerase assay. Anal Biochem 269: 403-409.
    • (1999) Anal Biochem , vol.269 , pp. 403-409
    • Roy, B.1    Beuneu, C.2    Roux, P.3    Buc, H.4    Lemaire, G.5    Lepoivre, M.6
  • 24
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP. 1996. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382: 325-331.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5
  • 25
    • 0142062498 scopus 로고    scopus 로고
    • Radicals with a controlled lifestyle
    • Stubbe J. 2003. Radicals with a controlled lifestyle. Chem Commun 2511-2513.
    • (2003) Chem Commun , pp. 2511-2513
    • Stubbe, J.1
  • 26
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase K, Dyson HJ, Wright PE. 2007. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447: 1021-1025.
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 27
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. 2002. Intrinsically unstructured proteins. Trends Biochem Sci 27: 527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 28
    • 0742288019 scopus 로고    scopus 로고
    • Global Gene Expression Responses of Fission Yeast to Ionizing Radiation
    • DOI 10.1091/mbc.E03-08-0569
    • Watson A, Mata J, Bahler J, Carr A, Humphrey T. 2004. Global gene expression responses of fission yeast to ionizing radiation. Mol Biol Cell 15: 851-860. (Pubitemid 38146498)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 851-860
    • Watson, A.1    Mata, J.2    Bahler, J.3    Carr, A.4    Humphrey, T.5
  • 29
    • 57349130603 scopus 로고    scopus 로고
    • Dif1 controls subcellular localization of ribonucleotide reductase by mediating nuclear import of the R2 subunit
    • Wu X, Huang M. 2008. Dif1 controls subcellular localization of ribonucleotide reductase by mediating nuclear import of the R2 subunit. Mol Cell Biol 28: 7156-7167.
    • (2008) Mol Cell Biol , vol.28 , pp. 7156-7167
    • Wu, X.1    Huang, M.2
  • 30
    • 31944444142 scopus 로고    scopus 로고
    • Nuclear localization of the Saccharomyces cerevisiae ribonucleotide reductase small subunit requires a karyopherin and a WD40 repeat protein
    • Zhang Z, An X, Yang K, Perlstein DL, Hicks L, Kelleher N, Stubbe J, Huang M. 2006. Nuclear localization of the Saccharomyces cerevisiae ribonucleotide reductase small subunit requires a karyopherin and a WD40 repeat protein. Proc Natl Acad Sci 103: 1422-1427.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 1422-1427
    • Zhang, Z.1    An, X.2    Yang, K.3    Perlstein, D.L.4    Hicks, L.5    Kelleher, N.6    Stubbe, J.7    Huang, M.8
  • 31
    • 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 104: 2217-2222.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 2217-2222
    • Zhang, Z.1    Yang, K.2    Chen, C.C.3    Feser, J.4    Huang, M.5
  • 32
    • 0037133566 scopus 로고    scopus 로고
    • The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1
    • Zhao X, Rothstein R. 2002. The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1. Proc Natl Acad Sci 99: 3746-3751.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 3746-3751
    • Zhao, X.1    Rothstein, R.2
  • 33
    • 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.
    • (1998) Mol Cell , vol.2 , pp. 329-340
    • Zhao, X.1    Muller, E.G.2    Rothstein, R.3
  • 34
    • 0034460153 scopus 로고    scopus 로고
    • Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality
    • Zhao X, Georgieva B, Chabes A, Domkin V, Ippel JH, Schleucher J, Wijmenga S, Thelander L, Rothstein R. 2000. Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality. Mol Cell Biol 20: 9076-9083.
    • (2000) Mol Cell Biol , vol.20 , pp. 9076-9083
    • Zhao, X.1    Georgieva, B.2    Chabes, A.3    Domkin, V.4    Ippel, J.H.5    Schleucher, J.6    Wijmenga, S.7    Thelander, L.8    Rothstein, R.9
  • 35
    • 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.
    • (2001) EMBO J , vol.20 , pp. 3544-3553
    • Zhao, X.1    Chabes, A.2    Domkin, V.3    Thelander, L.4    Rothstein, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.