메뉴 건너뛰기




Volumn 19, Issue 3, 2007, Pages 331-336

Elongator complex: how many roles does it play?

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; HOLOENZYME; PHOSPHOTRANSFERASE; RNA POLYMERASE II; TRANSCRIPTION ELONGATION FACTOR; TRANSFER RNA;

EID: 34250305505     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2007.04.005     Document Type: Review
Times cited : (138)

References (56)
  • 1
    • 33748314757 scopus 로고    scopus 로고
    • Breaking barriers to transcription elongation
    • Saunders A., Core L.J., and Lis J.T. Breaking barriers to transcription elongation. Nat Rev Mol Cell Biol 7 (2006) 557-567
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 557-567
    • Saunders, A.1    Core, L.J.2    Lis, J.T.3
  • 5
  • 6
    • 0032541670 scopus 로고    scopus 로고
    • IKAP is a scaffold protein of the IκB kinase complex
    • Cohen L., Henzel W.J., and Baeuerle P.A. IKAP is a scaffold protein of the IκB kinase complex. Nature 395 (1998) 292-296
    • (1998) Nature , vol.395 , pp. 292-296
    • Cohen, L.1    Henzel, W.J.2    Baeuerle, P.A.3
  • 7
    • 0037200023 scopus 로고    scopus 로고
    • A novel specific role for IκB kinase complex-associated protein in cytosolic stress signaling
    • Holmberg C., Katz S., Lerdrup M., Herdegen T., Jaattela M., Aronheim A., and Kallunki T. A novel specific role for IκB kinase complex-associated protein in cytosolic stress signaling. J Biol Chem 277 (2002) 31918-31928
    • (2002) J Biol Chem , vol.277 , pp. 31918-31928
    • Holmberg, C.1    Katz, S.2    Lerdrup, M.3    Herdegen, T.4    Jaattela, M.5    Aronheim, A.6    Kallunki, T.7
  • 8
    • 0036241663 scopus 로고    scopus 로고
    • Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo
    • Pokholok D.K., Hannett N.M., and Young R.A. Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo. Mol Cell 9 (2002) 799-809
    • (2002) Mol Cell , vol.9 , pp. 799-809
    • Pokholok, D.K.1    Hannett, N.M.2    Young, R.A.3
  • 9
    • 15244355534 scopus 로고    scopus 로고
    • Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation
    • Rahl P.B., Chen C.Z., and Collins R.N. Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation. Mol Cell 17 (2005) 841-853
    • (2005) Mol Cell , vol.17 , pp. 841-853
    • Rahl, P.B.1    Chen, C.Z.2    Collins, R.N.3
  • 10
    • 33749078546 scopus 로고    scopus 로고
    • Elevated levels of two tRNA species bypass the requirement for elongator complex in transcription and exocytosis
    • This paper provides evidence to support the idea that the cytoplasmic role of Elongator is in tRNA modification.
    • Esberg A., Huang B., Johansson M.J., and Bystrom A.S. Elevated levels of two tRNA species bypass the requirement for elongator complex in transcription and exocytosis. Mol Cell 24 (2006) 139-148. This paper provides evidence to support the idea that the cytoplasmic role of Elongator is in tRNA modification.
    • (2006) Mol Cell , vol.24 , pp. 139-148
    • Esberg, A.1    Huang, B.2    Johansson, M.J.3    Bystrom, A.S.4
  • 11
    • 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
    • Krogan N.J., and 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 (2001) 8203-8212
    • (2001) Mol Cell Biol , vol.21 , pp. 8203-8212
    • Krogan, N.J.1    Greenblatt, J.F.2
  • 13
    • 0037022226 scopus 로고    scopus 로고
    • Human Elongator facilitates RNA polymerase II transcription through chromatin
    • Kim J.H., Lane W.S., and Reinberg D. Human Elongator facilitates RNA polymerase II transcription through chromatin. Proc Natl Acad Sci U S A 99 (2002) 1241-1246
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1241-1246
    • Kim, J.H.1    Lane, W.S.2    Reinberg, D.3
  • 16
    • 0034724683 scopus 로고    scopus 로고
    • The Elp2 subunit of Elongator and elongating RNA polymerase II holoenzyme is a WD40 protein
    • Fellows J., Erdjument-Bromage H., Tempst P., and Svejstrup J. The Elp2 subunit of Elongator and elongating RNA polymerase II holoenzyme is a WD40 protein. J Biological Chem 275 (2000) 12896-12899
    • (2000) J Biological Chem , vol.275 , pp. 12896-12899
    • Fellows, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Svejstrup, J.4
  • 17
    • 0034660330 scopus 로고    scopus 로고
    • Overlapping roles for the histone acetyltransferase activities of SAGA and Elongator in vivo
    • Wittschieben B.O., Fellows J., Du W., Stillman D.J., and Svejstrup J.Q. Overlapping roles for the histone acetyltransferase activities of SAGA and Elongator in vivo. EMBO J 19 (2000) 3060-3068
    • (2000) EMBO J , vol.19 , pp. 3060-3068
    • Wittschieben, B.O.1    Fellows, J.2    Du, W.3    Stillman, D.J.4    Svejstrup, J.Q.5
  • 18
    • 2442425954 scopus 로고    scopus 로고
    • Elongator interactions with nascent mRNA revealed by RNA immunoprecipitation
    • Gilbert C., Kristjuhan A., Winkler G.S., and Svejstrup J.Q. Elongator interactions with nascent mRNA revealed by RNA immunoprecipitation. Mol Cell 14 (2004) 457-464
    • (2004) Mol Cell , vol.14 , pp. 457-464
    • Gilbert, C.1    Kristjuhan, A.2    Winkler, G.S.3    Svejstrup, J.Q.4
  • 19
    • 21244463476 scopus 로고    scopus 로고
    • Physical and functional interaction between elongator and the chromatin-associated Kt112 protein
    • This paper provides evidence that Elongator forms a fragile complex with the chromatin-associated Kti12 protein.
    • Petrakis T.G., Soegaard T.M., Erdjument-Bromage H., Tempst P., and Svejstrup J.Q. Physical and functional interaction between elongator and the chromatin-associated Kt112 protein. J Biol Chem 280 (2005) 19454-19460. This paper provides evidence that Elongator forms a fragile complex with the chromatin-associated Kti12 protein.
    • (2005) J Biol Chem , vol.280 , pp. 19454-19460
    • Petrakis, T.G.1    Soegaard, T.M.2    Erdjument-Bromage, H.3    Tempst, P.4    Svejstrup, J.Q.5
  • 20
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R., Penot G., Hubner M.R., Reid G., Brand H., Kos M., and Gannon F. Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115 (2003) 751-763
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 21
    • 13444292904 scopus 로고    scopus 로고
    • Histone modifications defining active genes persist after transcriptional and mitotic inactivation
    • This paper provides evidence that Elongator is found in the coding region, but not the promoter, of several genes.
    • Kouskouti A., and Talianidis I. Histone modifications defining active genes persist after transcriptional and mitotic inactivation. EMBO J 24 (2005) 347-357. This paper provides evidence that Elongator is found in the coding region, but not the promoter, of several genes.
    • (2005) EMBO J , vol.24 , pp. 347-357
    • Kouskouti, A.1    Talianidis, I.2
  • 22
    • 33745034833 scopus 로고    scopus 로고
    • Transcription impairment and cell migration defects in elongator-depleted cells: implication for familial dysautonomia
    • This paper provides evidence that Elongator is associated with the coding region of genes and that it affects histone acetylation and transcript elongation in human cells. Transcription defects may underlie familial dysautonomia.
    • Close P., Hawkes N., Cornez I., Creppe C., Lambert C.A., Rogister B., Siebenlist U., Merville M.P., Slaugenhaupt S.A., Bours V., et al. Transcription impairment and cell migration defects in elongator-depleted cells: implication for familial dysautonomia. Mol Cell 22 (2006) 521-531. This paper provides evidence that Elongator is associated with the coding region of genes and that it affects histone acetylation and transcript elongation in human cells. Transcription defects may underlie familial dysautonomia.
    • (2006) Mol Cell , vol.22 , pp. 521-531
    • Close, P.1    Hawkes, N.2    Cornez, I.3    Creppe, C.4    Lambert, C.A.5    Rogister, B.6    Siebenlist, U.7    Merville, M.P.8    Slaugenhaupt, S.A.9    Bours, V.10
  • 24
    • 0141454918 scopus 로고    scopus 로고
    • Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification
    • Fichtner L., Jablonowski D., Schierhorn A., Kitamoto H.K., Stark M.J., and Schaffrath R. Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49 (2003) 1297-1307
    • (2003) Mol Microbiol , vol.49 , pp. 1297-1307
    • Fichtner, L.1    Jablonowski, D.2    Schierhorn, A.3    Kitamoto, H.K.4    Stark, M.J.5    Schaffrath, R.6
  • 25
    • 15444371415 scopus 로고    scopus 로고
    • An early step in wobble uridine tRNA modification requires the Elongator complex
    • This paper provides the first evidence that Elongator might be involved in tRNA modification.
    • Huang B., Johansson M.J., and Bystrom A.S. An early step in wobble uridine tRNA modification requires the Elongator complex. Rna 11 (2005) 424-436. This paper provides the first evidence that Elongator might be involved in tRNA modification.
    • (2005) Rna , vol.11 , pp. 424-436
    • Huang, B.1    Johansson, M.J.2    Bystrom, A.S.3
  • 26
    • 0035901529 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin
    • Frohloff F., Fichtner L., Jablonowski D., Breunig K.D., and Schaffrath R. Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin. Embo J 20 (2001) 1993-2003
    • (2001) Embo J , vol.20 , pp. 1993-2003
    • Frohloff, F.1    Fichtner, L.2    Jablonowski, D.3    Breunig, K.D.4    Schaffrath, R.5
  • 27
    • 0035175582 scopus 로고    scopus 로고
    • Kluyveromyces lactis zymocin mode of action is linked to RNA polymerase II function via Elongator
    • Jablonowski D., Frohloff F., Fichtner L., Stark M.J., and Schaffrath R. Kluyveromyces lactis zymocin mode of action is linked to RNA polymerase II function via Elongator. Mol Microbiol 42 (2001) 1095-1105
    • (2001) Mol Microbiol , vol.42 , pp. 1095-1105
    • Jablonowski, D.1    Frohloff, F.2    Fichtner, L.3    Stark, M.J.4    Schaffrath, R.5
  • 28
    • 0035697437 scopus 로고    scopus 로고
    • Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin
    • Jablonowski D., Butler A.R., Fichtner L., Gardiner D., Schaffrath R., and Stark M.J. Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin. Genetics 159 (2001) 1479-1489
    • (2001) Genetics , vol.159 , pp. 1479-1489
    • Jablonowski, D.1    Butler, A.R.2    Fichtner, L.3    Gardiner, D.4    Schaffrath, R.5    Stark, M.J.6
  • 29
    • 0036267462 scopus 로고    scopus 로고
    • Molecular analysis of KTI12/TOT4, a Saccharomyces cerevisiae gene required for Kluyveromyces lactis zymocin action
    • Fichtner L., Frohloff F., Burkner K., Larsen M., Breunig K.D., and Schaffrath R. Molecular analysis of KTI12/TOT4, a Saccharomyces cerevisiae gene required for Kluyveromyces lactis zymocin action. Mol Microbiol 43 (2002) 783-791
    • (2002) Mol Microbiol , vol.43 , pp. 783-791
    • Fichtner, L.1    Frohloff, F.2    Burkner, K.3    Larsen, M.4    Breunig, K.D.5    Schaffrath, R.6
  • 30
    • 0036091217 scopus 로고    scopus 로고
    • KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin
    • Fichtner L., and Schaffrath R. KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44 (2002) 865-875
    • (2002) Mol Microbiol , vol.44 , pp. 865-875
    • Fichtner, L.1    Schaffrath, R.2
  • 31
    • 0037135604 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RNA polymerase II is affected by Kluyveromyces lactis zymocin
    • Jablonowski D., and Schaffrath R. Saccharomyces cerevisiae RNA polymerase II is affected by Kluyveromyces lactis zymocin. J Biol Chem 277 (2002) 26276-26280
    • (2002) J Biol Chem , vol.277 , pp. 26276-26280
    • Jablonowski, D.1    Schaffrath, R.2
  • 32
    • 0036360126 scopus 로고    scopus 로고
    • Protein interactions within Saccharomyces cerevisiae Elongator, a complex essential for Kluyveromyces lactis zymocicity
    • Fichtner L., Frohloff F., Jablonowski D., Stark M.J., and Schaffrath R. Protein interactions within Saccharomyces cerevisiae Elongator, a complex essential for Kluyveromyces lactis zymocicity. Mol Microbiol 45 (2002) 817-826
    • (2002) Mol Microbiol , vol.45 , pp. 817-826
    • Fichtner, L.1    Frohloff, F.2    Jablonowski, D.3    Stark, M.J.4    Schaffrath, R.5
  • 34
    • 0037428386 scopus 로고    scopus 로고
    • Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator (gamma-toxin target (TOT)) complex
    • Frohloff F., Jablonowski D., Fichtner L., and Schaffrath R. Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator (gamma-toxin target (TOT)) complex. J Biol Chem 278 (2003) 956-961
    • (2003) J Biol Chem , vol.278 , pp. 956-961
    • Frohloff, F.1    Jablonowski, D.2    Fichtner, L.3    Schaffrath, R.4
  • 35
    • 0038280146 scopus 로고    scopus 로고
    • 1 cell cycle arrest induced by Kluyveromyces lactis zymocin in budding yeast
    • 1 cell cycle arrest induced by Kluyveromyces lactis zymocin in budding yeast. Mol Genet Genomics 269 (2003) 188-196
    • (2003) Mol Genet Genomics , vol.269 , pp. 188-196
    • Mehlgarten, C.1    Schaffrath, R.2
  • 36
    • 1542373731 scopus 로고    scopus 로고
    • The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity
    • Jablonowski D., Fichtner L., Stark M.J., and Schaffrath R. The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity. Mol Biol Cell 15 (2004) 1459-1469
    • (2004) Mol Biol Cell , vol.15 , pp. 1459-1469
    • Jablonowski, D.1    Fichtner, L.2    Stark, M.J.3    Schaffrath, R.4
  • 37
    • 27144474752 scopus 로고    scopus 로고
    • The Kluyveromyces lactis γ-toxin targets tRNA anticodons
    • This paper provides evidence that the toxin zymocin kills Saccharomyces cerevisiae by targeting specific tRNA anticodons, whose modification requires Elongator.
    • Lu J., Huang B., Esberg A., Johansson M.J., and Bystrom A.S. The Kluyveromyces lactis γ-toxin targets tRNA anticodons. Rna 11 (2005) 1648-1654. This paper provides evidence that the toxin zymocin kills Saccharomyces cerevisiae by targeting specific tRNA anticodons, whose modification requires Elongator.
    • (2005) Rna , vol.11 , pp. 1648-1654
    • Lu, J.1    Huang, B.2    Esberg, A.3    Johansson, M.J.4    Bystrom, A.S.5
  • 38
    • 33645064276 scopus 로고    scopus 로고
    • tRNAGlu wobble uridine methylation by Trm9 identifies Elongator's key role for zymocin-induced cell death in yeast
    • Jablonowski D., Zink S., Mehlgarten C., Daum G., and Schaffrath R. tRNAGlu wobble uridine methylation by Trm9 identifies Elongator's key role for zymocin-induced cell death in yeast. Mol Microbiol 59 (2006) 677-688
    • (2006) Mol Microbiol , vol.59 , pp. 677-688
    • Jablonowski, D.1    Zink, S.2    Mehlgarten, C.3    Daum, G.4    Schaffrath, R.5
  • 39
    • 0035804653 scopus 로고    scopus 로고
    • Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in transcription elongation in vivo
    • Jona G., Wittschieben B.O., Svejstrup J.Q., and Gileadi O. Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in transcription elongation in vivo. Gene 267 (2001) 31-36
    • (2001) Gene , vol.267 , pp. 31-36
    • Jona, G.1    Wittschieben, B.O.2    Svejstrup, J.Q.3    Gileadi, O.4
  • 40
    • 0037155793 scopus 로고    scopus 로고
    • The Rpb9 subunit of RNA polymerase II binds transcription factor TFIIE and interferes with the SAGA and elongator histone acetyltransferases
    • Van Mullem V., Wery M., Werner M., Vandenhaute J., and Thuriaux P. The Rpb9 subunit of RNA polymerase II binds transcription factor TFIIE and interferes with the SAGA and elongator histone acetyltransferases. J Biol Chem 277 (2002) 10220-10225
    • (2002) J Biol Chem , vol.277 , pp. 10220-10225
    • Van Mullem, V.1    Wery, M.2    Werner, M.3    Vandenhaute, J.4    Thuriaux, P.5
  • 41
    • 14244267814 scopus 로고    scopus 로고
    • Interaction of Fcp1 phosphatase with elongating RNA polymerase II holoenzyme, enzymatic mechanism of action, and genetic interaction with elongator
    • Kong S.E., Kobor M.S., Krogan N.J., Somesh B.P., Sogaard T.M., Greenblatt J.F., and Svejstrup J.Q. Interaction of Fcp1 phosphatase with elongating RNA polymerase II holoenzyme, enzymatic mechanism of action, and genetic interaction with elongator. J Biol Chem 280 (2005) 4299-4306
    • (2005) J Biol Chem , vol.280 , pp. 4299-4306
    • Kong, S.E.1    Kobor, M.S.2    Krogan, N.J.3    Somesh, B.P.4    Sogaard, T.M.5    Greenblatt, J.F.6    Svejstrup, J.Q.7
  • 42
    • 33748648400 scopus 로고    scopus 로고
    • Mutations in ABO1/ELO2, a subunit of holo-Elongator, increase abscisic acid sensitivity and drought tolerance in Arabidopsis thaliana
    • Chen Z., Zhang H., Jablonowski D., Zhou X., Ren X., Hong X., Schaffrath R., Zhu J.K., and Gong Z. Mutations in ABO1/ELO2, a subunit of holo-Elongator, increase abscisic acid sensitivity and drought tolerance in Arabidopsis thaliana. Mol Cell Biol 26 (2006) 6902-6912
    • (2006) Mol Cell Biol , vol.26 , pp. 6902-6912
    • Chen, Z.1    Zhang, H.2    Jablonowski, D.3    Zhou, X.4    Ren, X.5    Hong, X.6    Schaffrath, R.7    Zhu, J.K.8    Gong, Z.9
  • 45
    • 1442328913 scopus 로고    scopus 로고
    • Familial dysautonomia
    • Axelrod F.B. Familial dysautonomia. Muscle Nerve 29 (2004) 352-363
    • (2004) Muscle Nerve , vol.29 , pp. 352-363
    • Axelrod, F.B.1
  • 50
    • 3543038157 scopus 로고    scopus 로고
    • Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-elongator
    • Petrakis T.G., Wittschieben B.O., and Svejstrup J.Q. Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-elongator. J Biol Chem 279 (2004) 32087-32092
    • (2004) J Biol Chem , vol.279 , pp. 32087-32092
    • Petrakis, T.G.1    Wittschieben, B.O.2    Svejstrup, J.Q.3
  • 51
    • 0141953237 scopus 로고    scopus 로고
    • Cytoskeletal dynamics and transport in growth cone motility and axon guidance
    • Dent E.W., and Gertler F.B. Cytoskeletal dynamics and transport in growth cone motility and axon guidance. Neuron 40 (2003) 209-227
    • (2003) Neuron , vol.40 , pp. 209-227
    • Dent, E.W.1    Gertler, F.B.2
  • 52
    • 0036719449 scopus 로고    scopus 로고
    • Breaking the neuronal sphere: regulation of the actin cytoskeleton in neuritogenesis
    • da Silva J.S., and Dotti C.G. Breaking the neuronal sphere: regulation of the actin cytoskeleton in neuritogenesis. Nat Rev Neurosci 3 (2002) 694-704
    • (2002) Nat Rev Neurosci , vol.3 , pp. 694-704
    • da Silva, J.S.1    Dotti, C.G.2
  • 53
    • 0242285769 scopus 로고    scopus 로고
    • Global control of gene expression in yeast by the Ccr4-Not complex
    • Collart M.A. Global control of gene expression in yeast by the Ccr4-Not complex. Gene 313 (2003) 1-16
    • (2003) Gene , vol.313 , pp. 1-16
    • Collart, M.A.1
  • 54
    • 1542315317 scopus 로고    scopus 로고
    • Antiviral protein Ski8 is a direct partner of Spo11 in meiotic DNA break formation, independent of its cytoplasmic role in RNA metabolism
    • Arora C., Kee K., Maleki S., and Keeney S. Antiviral protein Ski8 is a direct partner of Spo11 in meiotic DNA break formation, independent of its cytoplasmic role in RNA metabolism. Mol Cell 13 (2004) 549-559
    • (2004) Mol Cell , vol.13 , pp. 549-559
    • Arora, C.1    Kee, K.2    Maleki, S.3    Keeney, S.4
  • 55
    • 0036495007 scopus 로고    scopus 로고
    • A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?
    • Chinenov Y. A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?. Trends Biochem Sci 27 (2002) 115-117
    • (2002) Trends Biochem Sci , vol.27 , pp. 115-117
    • Chinenov, Y.1
  • 56
    • 33645070795 scopus 로고    scopus 로고
    • The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine
    • Paraskevopoulou C., Fairhurst S.A., Lowe D.J., Brick P., and Onesti S. The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine. Mol Microbiol 59 (2006) 795-806
    • (2006) Mol Microbiol , vol.59 , pp. 795-806
    • Paraskevopoulou, C.1    Fairhurst, S.A.2    Lowe, D.J.3    Brick, P.4    Onesti, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.