메뉴 건너뛰기




Volumn 19, Issue 3, 2012, Pages 314-320

The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; HISTONE ACETYLTRANSFERASE; PROTEIN ELP4; PROTEIN ELP456; PROTEIN ELP5; PROTEIN ELP6; RECA PROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84858000251     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2234     Document Type: Article
Times cited : (78)

References (42)
  • 2
    • 15244355534 scopus 로고    scopus 로고
    • Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation
    • DOI 10.1016/j.molcel.2005.02.018
    • Rahl, P.B., Chen, C.Z. & Collins, R.N. Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation. Mol. Cell 17, 841-853 (2005). (Pubitemid 40386945)
    • (2005) Molecular Cell , vol.17 , Issue.6 , pp. 841-853
    • Rahl, P.B.1    Chen, C.Z.2    Collins, R.N.3
  • 3
    • 59349089711 scopus 로고    scopus 로고
    • Elongator controls the migration and differentiation of cortical neurons through acetylation of α-tubulin
    • Creppe, C. et al. Elongator controls the migration and differentiation of cortical neurons through acetylation of α-tubulin. Cell 136, 551-564 (2009).
    • (2009) Cell , vol.136 , pp. 551-564
    • Creppe, C.1
  • 4
    • 73349133725 scopus 로고    scopus 로고
    • The Elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents
    • Li, Q. et al. The Elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents. PLoS Genet. 5, e1000684 (2009).
    • (2009) PLoS Genet. , vol.5
    • Li, Q.1
  • 5
    • 75749142980 scopus 로고    scopus 로고
    • A role for the Elongator complex in zygotic paternal genome demethylation
    • Okada, Y., Yamagata, K., Hong, K., Wakayama, T. & Zhang, Y. A role for the Elongator complex in zygotic paternal genome demethylation. Nature 463, 554-558 (2010).
    • (2010) Nature , vol.463 , pp. 554-558
    • Okada, Y.1    Yamagata, K.2    Hong, K.3    Wakayama, T.4    Zhang, Y.5
  • 6
    • 33749078546 scopus 로고    scopus 로고
    • Elevated Levels of Two tRNA Species Bypass the Requirement for Elongator Complex in Transcription and Exocytosis
    • DOI 10.1016/j.molcel.2006.07.031, PII S1097276506005338
    • Esberg, A., Huang, B., Johansson, M.J.O. & Bystrom, A.S. Elevated levels of two tRNA species bypass the requirement for elongator complex in transcription and exocytosis. Mol. Cell 24, 139-148 (2006). (Pubitemid 44466676)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 139-148
    • Esberg, A.1    Huang, B.2    Johansson, M.J.O.3    Bystrom, A.S.4
  • 7
    • 15444371415 scopus 로고    scopus 로고
    • An early step in wobble uridine tRNA modification requires the Elongator complex
    • DOI 10.1261/rna.7247705
    • Huang, B., Johansson, M.J.O. & Bystrom, A.S. An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11, 424-436 (2005). (Pubitemid 40397176)
    • (2005) RNA , vol.11 , Issue.4 , pp. 424-436
    • Huang, B.1    Johansson, M.J.O.2    Bystrom, A.S.3
  • 8
    • 71849108697 scopus 로고    scopus 로고
    • Deciphering synonymous codons in the three domains of life: Co-evolution with specific tRNA modification enzymes
    • Grosjean, H., de Crecy-Lagard, V. & Marck, C. Deciphering synonymous codons in the three domains of life: co-evolution with specific tRNA modification enzymes. FEBS Lett. 584, 252-264 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 252-264
    • Grosjean, H.1    De Crecy-Lagard, V.2    Marck, C.3
  • 9
    • 52949102950 scopus 로고    scopus 로고
    • A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae
    • Huang, B., Lu, J. & Bystrom, A.S. A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2- thiouridine in Saccharomyces cerevisiae. RNA 14, 2183-2194 (2008).
    • (2008) RNA , vol.14 , pp. 2183-2194
    • Huang, B.1    Lu, J.2    Bystrom, A.S.3
  • 10
    • 43249104840 scopus 로고    scopus 로고
    • Eukaryotic wobble uridine modifications promote a functionally redundant decoding system
    • DOI 10.1128/MCB.01542-07
    • Johansson, M.J.O., Esberg, A., Huang, B., Bjork, G.R. & Bystrom, A.S. Eukaryotic wobble uridine modifications promote a functionally redundant decoding system. Mol. Cell. Biol. 28, 3301-3312 (2008). (Pubitemid 351657094)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.10 , pp. 3301-3312
    • Johansson, M.J.O.1    Esberg, A.2    Huang, B.3    Bjork, G.R.4    Bystrom, A.S.5
  • 13
    • 0035171624 scopus 로고    scopus 로고
    • Characterization of a six-subunit Holo-Elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae
    • DOI 10.1128/MCB.21.23.8203-8212.2001
    • Krogan, N.J. & Greenblatt, J.F. Characterization of a six-subunit holo-elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 21, 8203-8212 (2001). (Pubitemid 33051809)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.23 , pp. 8203-8212
    • Krogan, N.J.1    Greenblatt, J.F.2
  • 15
    • 0035901529 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin
    • DOI 10.1093/emboj/20.8.1993
    • Frohloff, F., Fichtner, L., Jablonowski, D., Breunig, K.D. & Schaffrath, R. Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin. EMBO J. 20, 1993-2003 (2001). (Pubitemid 32397401)
    • (2001) EMBO Journal , vol.20 , Issue.8 , pp. 1993-2003
    • Frohloff, F.1    Fichtner, L.2    Jablonowski, D.3    Breunig, K.D.4    Schaffrath, R.5
  • 16
    • 77952791647 scopus 로고    scopus 로고
    • Elongator function in tRNA wobble uridine modification is conserved between yeast and plants
    • Mehlgarten, C. et al. Elongator function in tRNA wobble uridine modification is conserved between yeast and plants. Mol. Microbiol. 76, 1082-1094 (2010).
    • (2010) Mol. Microbiol. , vol.76 , pp. 1082-1094
    • Mehlgarten, C.1
  • 17
    • 68249089400 scopus 로고    scopus 로고
    • Defects in tRNA modification associated with neurological and developmental dysfunctions in Caenorhabditis elegans Elongator mutants
    • Chen, C., Tuck, S. & Bystrom, A.S. Defects in tRNA modification associated with neurological and developmental dysfunctions in Caenorhabditis elegans Elongator mutants. PLoS Genet. 5, e1000561 (2009).
    • (2009) PLoS Genet. , vol.5
    • Chen, C.1    Tuck, S.2    Bystrom, A.S.3
  • 19
    • 58749097964 scopus 로고    scopus 로고
    • Variants of the elongator protein 3 (ELP3) gene are associated with motor neuron degeneration
    • Simpson, C.L. et al. Variants of the elongator protein 3 (ELP3) gene are associated with motor neuron degeneration. Hum. Mol. Genet. 18, 472-481 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 472-481
    • Simpson, C.L.1
  • 20
    • 69249246953 scopus 로고    scopus 로고
    • Centrotemporal sharp wave EEG trait in rolandic epilepsy maps to Elongator protein complex 4 (ELP4)
    • Strug, L.J. et al. Centrotemporal sharp wave EEG trait in rolandic epilepsy maps to Elongator protein complex 4 (ELP4). Eur. J. Hum. Genet. 17, 1171-1181 (2009).
    • (2009) Eur. J. Hum. Genet. , vol.17 , pp. 1171-1181
    • Strug, L.J.1
  • 21
    • 0033564627 scopus 로고    scopus 로고
    • Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin
    • DOI 10.1093/emboj/18.12.3451
    • Salgado-Garrido, J., Bragado-Nilsson, E., Kandels-Lewis, S. & Seraphin, B. Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. EMBO J. 18, 3451-3462 (1999). (Pubitemid 29276590)
    • (1999) EMBO Journal , vol.18 , Issue.12 , pp. 3451-3462
    • Salgado-Garrido, J.1    Bragado-Nilsson, E.2    Kandels-Lewis, S.3    Seraphin, B.4
  • 22
  • 23
    • 0026500416 scopus 로고
    • The structure of the Escherichia coli RecA protein monomer and polymer
    • Story, R.M., Weber, I.T. & Steitz, T.A. The structure of the Escherichia coli RecA protein monomer and polymer. Nature 355, 318-325 (1992).
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 24
    • 70350344051 scopus 로고    scopus 로고
    • Running in reverse: The structural basis for translocation polarity in hexameric helicases
    • Thomsen, N.D. & Berger, J.M. Running in reverse: the structural basis for translocation polarity in hexameric helicases. Cell 139, 523-534 (2009).
    • (2009) Cell , vol.139 , pp. 523-534
    • Thomsen, N.D.1    Berger, J.M.2
  • 25
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton, M.R., Sawaya, M.R., Ellenberger, T. & Wigley, D.B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101, 589-600 (2000).
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 26
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M.R., Dillingham, M.S. & Wigley, D.B. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76, 23-50 (2007).
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 27
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • DOI 10.1038/nature04943, PII NATURE04943
    • Enemark, E.J. & Joshua-Tor, L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 442, 270-275 (2006). (Pubitemid 44114897)
    • (2006) Nature , vol.442 , Issue.7100 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 28
    • 0023664161 scopus 로고
    • RecA protein-promoted ATP hydrolysis occurs throughout RecA nucleoprotein filaments
    • Brenner, S.L. et al. RecA protein-promoted ATP hydrolysis occurs throughout RecA nucleoprotein filaments. J. Biol. Chem. 262, 4011-4016 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 4011-4016
    • Brenner, S.L.1
  • 29
    • 0019818718 scopus 로고
    • Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Characterization of ATP hydrolysis
    • Weinstock, G.M., McEntee, K. & Lehman, I.R. Hydrolysis of nucleoside triphosphates catalyzed by the RecA protein of Escherichia coli. Characterization of ATP hydrolysis. J. Biol. Chem. 256, 8829-8834 (1981). (Pubitemid 12229898)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.16 , pp. 8829-8834
    • Weinstock, G.M.1    McEntee, K.2    Lehman, I.R.3
  • 30
    • 0019960564 scopus 로고
    • Rho Factors from polarity suppressor mutants with defects in their RNA interactions
    • Richardson, J.P. & Carey, J.L. III. rho Factors from polarity suppressor mutants with defects in their RNA interactions. J. Biol. Chem. 257, 5767-5771 (1982). (Pubitemid 12015938)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.10 , pp. 5767-5771
    • Richardson, J.P.1    Carey III, J.L.2
  • 31
    • 0019845187 scopus 로고
    • Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Hydrolysis of UTP
    • Weinstock, G.M., McEntee, K. & Lehman, I.R. Hydrolysis of nucleoside triphosphates catalyzed by the RecA protein of Escherichia coli. Hydrolysis of UTP. J. Biol. Chem. 256, 8856-8858 (1981). (Pubitemid 12229902)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.16 , pp. 8856-8858
    • Weinstock, G.M.1    McEntee, K.2    Lehman, I.R.3
  • 32
    • 0017582694 scopus 로고
    • Characterization of the nucleoside triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor rho. I. Enzymatic properties and effects of inhibitors
    • Lowery, C. & Richardson, J.P. Characterization of the nucleoside triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor p. I. Enzymatic properties and effects of inhibitors. J. Biol. Chem. 252, 1375-1380 (1977). (Pubitemid 8047900)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.4 , pp. 1375-1380
    • Lowery, C.1    Richardson, J.P.2
  • 33
    • 0028997105 scopus 로고
    • Sm and Sm-like proteins belong to a large family: Identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs
    • Séraphin, B. Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs. EMBO J. 14, 2089-2098 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2089-2098
    • Séraphin, B.1
  • 35
    • 0028103275 scopus 로고
    • The Ccp4 suite-programs for protein crystallography
    • CCP4
    • CCP4. The Ccp4 suite-programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 36
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • DOI 10.1016/S0076-6879(97)76073-7
    • Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997). (Pubitemid 27085618)
    • (1997) Methods in Enzymology , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 38
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I.W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383 (2007).
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1
  • 40
    • 0028275669 scopus 로고
    • Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent
    • Baudin, F., Bach, C., Cusack, S. & Ruigrok, R.W. Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent. EMBO J. 13, 3158-3165 (1994). (Pubitemid 24213467)
    • (1994) EMBO Journal , vol.13 , Issue.13 , pp. 3158-3165
    • Baudin, F.1    Bach, C.2    Cusack, S.3    Ruigrok, R.W.H.4
  • 42
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • DOI 10.1038/13732
    • Rigaut, G. et al. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032 (1999). (Pubitemid 29474865)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.