메뉴 건너뛰기




Volumn 128, Issue 2, 2009, Pages 206-217

Correlation between recombinase activating gene 1 ubiquitin ligase activity and V(D)J recombination

Author keywords

CDC34; Recombinase activating gene 1; Ubiquitin ligase; V(D)J recombination

Indexed keywords

CDC34 ENZYME; LYSINE; RAG1 PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 69949131788     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/j.1365-2567.2009.03101.x     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 0028237683 scopus 로고
    • Definition of a core region of RAG-2 that is functional in V(D)J recombination
    • Sadofsky MJ, Hesse JE, Gellert M. Definition of a core region of RAG-2 that is functional in V(D)J recombination. Nucleic Acids Res 1994 22 : 1805 1809.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1805-1809
    • Sadofsky, M.J.1    Hesse, J.E.2    Gellert, M.3
  • 2
    • 0027770854 scopus 로고
    • Expression and V(D)J recombination activity of mutated RAG-1 proteins
    • Sadofsky MJ, Hesse JE, McBlane JF, Gellert M. Expression and V(D)J recombination activity of mutated RAG-1 proteins. Nucleic Acids Res 1993 21 : 5644 5650.
    • (1993) Nucleic Acids Res , vol.21 , pp. 5644-5650
    • Sadofsky, M.J.1    Hesse, J.E.2    McBlane, J.F.3    Gellert, M.4
  • 3
    • 0027197151 scopus 로고
    • Dispensable sequence motifs in the RAG-1 and RAG-2 genes for plasmid V(D)J recombination
    • Silver DP, Spanopoulou E, Mulligan RC, Baltimore D. Dispensable sequence motifs in the RAG-1 and RAG-2 genes for plasmid V(D)J recombination. Proc Natl Acad Sci USA 1993 90 : 6100 6104.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6100-6104
    • Silver, D.P.1    Spanopoulou, E.2    Mulligan, R.C.3    Baltimore, D.4
  • 5
    • 0030871602 scopus 로고    scopus 로고
    • Complementation of V(D)J recombination deficiency in RAG-1(---) B cells reveals a requirement for novel elements in the N-terminus of RAG-1
    • Roman CA, Cherry SR, Baltimore D. Complementation of V(D)J recombination deficiency in RAG-1(---) B cells reveals a requirement for novel elements in the N-terminus of RAG-1. Immunity 1997 7 : 13 24.
    • (1997) Immunity , vol.7 , pp. 13-24
    • Roman, C.A.1    Cherry, S.R.2    Baltimore, D.3
  • 6
    • 40049107888 scopus 로고    scopus 로고
    • Biochemical and folding defects in a RAG1 variant associated with Omenn syndrome
    • Simkus C, Anand P, Bhattacharyya A, Jones JM. Biochemical and folding defects in a RAG1 variant associated with Omenn syndrome. J Immunol 2007 179 : 8332 8340.
    • (2007) J Immunol , vol.179 , pp. 8332-8340
    • Simkus, C.1    Anand, P.2    Bhattacharyya, A.3    Jones, J.M.4
  • 7
    • 43249105936 scopus 로고    scopus 로고
    • An immunodeficiency disease with RAG mutations and granulomas
    • Schuetz C, Huck K, Gudowius S et al. An immunodeficiency disease with RAG mutations and granulomas. N Engl J Med 2008 358 : 2030 2038.
    • (2008) N Engl J Med , vol.358 , pp. 2030-2038
    • Schuetz, C.1    Huck, K.2    Gudowius, S.3
  • 8
    • 0035161258 scopus 로고    scopus 로고
    • V(D)J recombination defects in lymphocytes due to RAG mutations: Severe immunodeficiency with a spectrum of clinical presentations
    • Villa A, Sobacchi C, Notarangelo LD et al. V(D)J recombination defects in lymphocytes due to RAG mutations: severe immunodeficiency with a spectrum of clinical presentations. Blood 2001 97 : 81 8.
    • (2001) Blood , vol.97 , pp. 81-8
    • Villa, A.1    Sobacchi, C.2    Notarangelo, L.D.3
  • 9
    • 0018992813 scopus 로고
    • ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation
    • Ciechanover A, Heller H, Elias S, Haas AL, Hershko A. ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proc Natl Acad Sci USA 1980 77 : 1365 1368.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1365-1368
    • Ciechanover, A.1    Heller, H.2    Elias, S.3    Haas, A.L.4    Hershko, A.5
  • 10
    • 0019000271 scopus 로고
    • Proposed role of ATP in protein breakdown: Conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis
    • Hershko A, Ciechanover A, Heller H, Haas AL, Rose IA. Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc Natl Acad Sci USA 1980 77 : 1783 1786.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1783-1786
    • Hershko, A.1    Ciechanover, A.2    Heller, H.3    Haas, A.L.4    Rose, I.A.5
  • 11
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart CM. Back to the future with ubiquitin. Cell 2004 116 : 181 190.
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 12
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko A, Heller H, Elias S, Ciechanover A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J Biol Chem 1983 258 : 8206 8214.
    • (1983) J Biol Chem , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 13
    • 0034604341 scopus 로고    scopus 로고
    • Regulation of transcription by ubiquitination without proteolysis: Cdc34-SCF(Met30)-mediated inactivation of the transcription factor Met4
    • Kaiser P, Flick K, Wittenberg C, Reed SI. Regulation of transcription by ubiquitination without proteolysis: Cdc34-SCF(Met30)-mediated inactivation of the transcription factor Met4. Cell 2000 102 : 303 314.
    • (2000) Cell , vol.102 , pp. 303-314
    • Kaiser, P.1    Flick, K.2    Wittenberg, C.3    Reed, S.I.4
  • 14
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence J, Gali RR, Dittmar G, Sherman F, Karin M, Finley D. Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell 2000 102 : 67 76.
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gali, R.R.2    Dittmar, G.3    Sherman, F.4    Karin, M.5    Finley, D.6
  • 15
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J, Sadis S, Haas AL, Finley D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 1995 15 : 1265 1273.
    • (1995) Mol Cell Biol , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 16
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W, Walz J, Zuhl F, Seemuller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 1998 92 : 367 380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 17
    • 20444403003 scopus 로고    scopus 로고
    • Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle
    • Jiang H, Chang FC, Ross AE, Lee J, Nakayama K, Nakayama K, Desiderio S. Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle. Mol Cell 2005 18 : 699 709.
    • (2005) Mol Cell , vol.18 , pp. 699-709
    • Jiang, H.1    Chang, F.C.2    Ross, A.E.3    Lee, J.4    Nakayama, K.5    Nakayama, K.6    Desiderio, S.7
  • 18
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney JD, Hochstrasser M. Substrate targeting in the ubiquitin system. Cell 1999 97 : 427 430.
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 19
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci USA 1995 92 : 5249.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5249
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 21
    • 28944435024 scopus 로고    scopus 로고
    • Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCF-Cdc34
    • Petroski MD, Deshaies RJ. Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCF-Cdc34. Cell 2005 123 : 1107 1120.
    • (2005) Cell , vol.123 , pp. 1107-1120
    • Petroski, M.D.1    Deshaies, R.J.2
  • 22
    • 0347994908 scopus 로고    scopus 로고
    • Autoubiquitylation of the V(D)J recombinase protein RAG1
    • Jones JM, Gellert M. Autoubiquitylation of the V(D)J recombinase protein RAG1. Proc Natl Acad Sci USA 2003 100 : 15446 15451.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15446-15451
    • Jones, J.M.1    Gellert, M.2
  • 23
    • 0037335702 scopus 로고    scopus 로고
    • The RAG1 N-terminal domain is an E3 ubiquitin ligase
    • Yurchenko V, Xue Z, Sadofsky M. The RAG1 N-terminal domain is an E3 ubiquitin ligase. Genes Dev 2003 17 : 581 585.
    • (2003) Genes Dev , vol.17 , pp. 581-585
    • Yurchenko, V.1    Xue, Z.2    Sadofsky, M.3
  • 24
    • 0030959658 scopus 로고    scopus 로고
    • Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster
    • Bellon SF, Rodgers KK, Schatz DG, Coleman JE, Steitz TA. Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat Struct Biol 1997 4 : 586 591.
    • (1997) Nat Struct Biol , vol.4 , pp. 586-591
    • Bellon, S.F.1    Rodgers, K.K.2    Schatz, D.G.3    Coleman, J.E.4    Steitz, T.A.5
  • 26
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N, Wang P, Jeffrey PD, Pavletich NP. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 2000 102 : 533 539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 27
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm M, Shevchenko A, Houthaeve T, Breit S, Schweigerer L, Fotsis T, Mann M. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 1996 379 : 466 469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 28
    • 62749159936 scopus 로고    scopus 로고
    • Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase
    • doi:.
    • Simkus C, Mayika M, Jones JM. Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase. Mol Immunol 2009 46 : 1319 1325. doi :.
    • (2009) Mol Immunol , vol.46 , pp. 1319-1325
    • Simkus, C.1    Mayika, M.2    Jones, J.M.3
  • 29
    • 0023659483 scopus 로고
    • Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J joining signals
    • Hesse JE, Lieber MR, Gellert M, Mizuuchi K. Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J joining signals. Cell 1987 49 : 775 783.
    • (1987) Cell , vol.49 , pp. 775-783
    • Hesse, J.E.1    Lieber, M.R.2    Gellert, M.3    Mizuuchi, K.4
  • 30
    • 21244493533 scopus 로고    scopus 로고
    • The unique region of surrogate light chain component lambda5 is a heavy chain-specific regulator of precursor B cell receptor signaling
    • Guloglu FB, Bajor E, Smith BP, Roman CA. The unique region of surrogate light chain component lambda5 is a heavy chain-specific regulator of precursor B cell receptor signaling. J Immunol 2005 175 : 358 366.
    • (2005) J Immunol , vol.175 , pp. 358-366
    • Guloglu, F.B.1    Bajor, E.2    Smith, B.P.3    Roman, C.A.4
  • 31
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superimpose protein coordinates
    • Cohen GE. ALIGN: a program to superimpose protein coordinates. J Appl Crystallogr 1997 30 : 1160 1161.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 32
    • 33947243954 scopus 로고    scopus 로고
    • A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate
    • Li W, Tu D, Brunger AT, Ye Y. A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate. Nature 2007 446 : 333 337.
    • (2007) Nature , vol.446 , pp. 333-337
    • Li, W.1    Tu, D.2    Brunger, A.T.3    Ye, Y.4
  • 33
    • 27144495057 scopus 로고    scopus 로고
    • E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer
    • Eletr ZM, Huang DT, Duda DM, Schulman BA, Kuhlman B. E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer. Nat Struct Mol Biol 2005 12 : 933 934.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 933-934
    • Eletr, Z.M.1    Huang, D.T.2    Duda, D.M.3    Schulman, B.A.4    Kuhlman, B.5
  • 34
    • 35148869981 scopus 로고    scopus 로고
    • Human Cdc34 employs distinct sites to coordinate attachment of ubiquitin to a substrate and assembly of polyubiquitin chains
    • Gazdoiu S, Yamoah K, Wu K, Pan ZQ. Human Cdc34 employs distinct sites to coordinate attachment of ubiquitin to a substrate and assembly of polyubiquitin chains. Mol Cell Biol 2007 27 : 7041 7052.
    • (2007) Mol Cell Biol , vol.27 , pp. 7041-7052
    • Gazdoiu, S.1    Yamoah, K.2    Wu, K.3    Pan, Z.Q.4
  • 36
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001 70 : 503 533.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 37
    • 0034791090 scopus 로고    scopus 로고
    • Ubiquitin enters the new millennium
    • Pickart CM. Ubiquitin enters the new millennium. Mol Cell 2001 8 : 499 504.
    • (2001) Mol Cell , vol.8 , pp. 499-504
    • Pickart, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.