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Volumn 23, Issue 2, 2013, Pages 235-242

Structural insights into Elongator function

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATOR COMPLEX; ELONGATOR PROTEIN; ELONGATOR PROTEIN 1; ELONGATOR PROTEIN 2; ELONGATOR PROTEIN 3; ELONGATOR PROTEIN 4; ELONGATOR PROTEIN 5; ELONGATOR PROTEIN 6; PROTEIN; RNA POLYMERASE II; TRANSCRIPTION ELONGATION FACTOR; TRANSFER RNA; UNCLASSIFIED DRUG; URIDINE;

EID: 84878526158     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2013.02.009     Document Type: Review
Times cited : (53)

References (57)
  • 5
    • 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., Collins R.N. Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation. Mol Cell 2005, 17:841-853.
    • (2005) Mol Cell , vol.17 , pp. 841-853
    • Rahl, P.B.1    Chen, C.Z.2    Collins, R.N.3
  • 6
    • 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 2010, 463:554-558.
    • (2010) Nature , vol.463 , pp. 554-558
    • Okada, Y.1    Yamagata, K.2    Hong, K.3    Wakayama, T.4    Zhang, Y.5
  • 7
    • 73349133725 scopus 로고    scopus 로고
    • The Elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents
    • Li Q., Fazly A.M., Zhou H., Huang S., Zhang Z., Stillman B. The Elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents. PLoS Genet 2009, 5:e1000684.
    • (2009) PLoS Genet , vol.5
    • Li, Q.1    Fazly, A.M.2    Zhou, H.3    Huang, S.4    Zhang, Z.5    Stillman, B.6
  • 8
    • 33749078546 scopus 로고    scopus 로고
    • Elevated levels of two tRNA species bypass the requirement for Elongator complex in transcription and exocytosis
    • Esberg A., Huang B., Johansson M.J., Bystrom A.S. Elevated levels of two tRNA species bypass the requirement for Elongator complex in transcription and exocytosis. Mol Cell 2006, 24:139-148.
    • (2006) Mol Cell , vol.24 , pp. 139-148
    • Esberg, A.1    Huang, B.2    Johansson, M.J.3    Bystrom, A.S.4
  • 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 2008, 14:2183-2194.
    • (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
    • Johansson M.J., Esberg A., Huang B., Bjork G.R., Bystrom A.S. Eukaryotic wobble uridine modifications promote a functionally redundant decoding system. Mol Cell Biol 2008, 28:3301-3312.
    • (2008) Mol Cell Biol , vol.28 , pp. 3301-3312
    • Johansson, M.J.1    Esberg, A.2    Huang, B.3    Bjork, G.R.4    Bystrom, A.S.5
  • 11
    • 84857367382 scopus 로고    scopus 로고
    • Human tRNA(Lys3)(UUU) is pre-structured by natural modifications for cognate and wobble codon binding through keto-enol tautomerism
    • Vendeix F.A., Murphy F.Vt., Cantara W.A., Leszczynska G., Gustilo E.M., Sproat B., Malkiewicz A., Agris P.F. Human tRNA(Lys3)(UUU) is pre-structured by natural modifications for cognate and wobble codon binding through keto-enol tautomerism. J Mol Biol 2012, 416:467-485.
    • (2012) J Mol Biol , vol.416 , pp. 467-485
    • Vendeix, F.A.1    Murphy, F.2    Cantara, W.A.3    Leszczynska, G.4    Gustilo, E.M.5    Sproat, B.6    Malkiewicz, A.7    Agris, P.F.8
  • 13
    • 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., Schaffrath R. Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin. EMBO J 2001, 20:1993-2003.
    • (2001) EMBO J , vol.20 , pp. 1993-2003
    • Frohloff, F.1    Fichtner, L.2    Jablonowski, D.3    Breunig, K.D.4    Schaffrath, R.5
  • 14
    • 27144474752 scopus 로고    scopus 로고
    • The Kluyveromyces lactis gamma-toxin targets tRNA anticodons
    • Lu J., Huang B., Esberg A., Johansson M.J., Bystrom A.S. The Kluyveromyces lactis gamma-toxin targets tRNA anticodons. RNA 2005, 11:1648-1654.
    • (2005) RNA , vol.11 , pp. 1648-1654
    • Lu, J.1    Huang, B.2    Esberg, A.3    Johansson, M.J.4    Bystrom, A.S.5
  • 15
    • 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., Young R.A. Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo. Mol Cell 2002, 9:799-809.
    • (2002) Mol Cell , vol.9 , pp. 799-809
    • Pokholok, D.K.1    Hannett, N.M.2    Young, R.A.3
  • 16
    • 34250305505 scopus 로고    scopus 로고
    • Elongator complex: how many roles does it play?
    • Svejstrup J.Q. Elongator complex: how many roles does it play?. Curr Opin Cell Biol 2007, 19:331-336.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 331-336
    • Svejstrup, J.Q.1
  • 18
    • 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., 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 2001, 21:8203-8212.
    • (2001) Mol Cell Biol , vol.21 , pp. 8203-8212
    • Krogan, N.J.1    Greenblatt, J.F.2
  • 21
    • 15444371415 scopus 로고    scopus 로고
    • An early step in wobble uridine tRNA modification requires the Elongator complex
    • Huang B., Johansson M.J.O., Bystrom A.S. An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 2005, 11:424-436.
    • (2005) RNA , vol.11 , pp. 424-436
    • Huang, B.1    Johansson, M.J.O.2    Bystrom, A.S.3
  • 23
    • 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 2009, 5:e1000561.
    • (2009) PLoS Genet , vol.5
    • Chen, C.1    Tuck, S.2    Bystrom, A.S.3
  • 24
    • 78651267261 scopus 로고    scopus 로고
    • The histone acetyltransferase Elp3 plays in active role in the control of synaptic bouton expansion and sleep in Drosophila
    • Singh N., Lorbeck M.T., Zervos A., Zimmerman J., Elefant F. The histone acetyltransferase Elp3 plays in active role in the control of synaptic bouton expansion and sleep in Drosophila. J Neurochem 2010, 115:493-504.
    • (2010) J Neurochem , vol.115 , pp. 493-504
    • Singh, N.1    Lorbeck, M.T.2    Zervos, A.3    Zimmerman, J.4    Elefant, F.5
  • 25
    • 79955380420 scopus 로고    scopus 로고
    • Role of Elongator subunit Elp3 in Drosophila melanogaster larval development and immunity
    • Walker J., Kwon S.Y., Badenhorst P., East P., McNeill H., Svejstrup J.Q. Role of Elongator subunit Elp3 in Drosophila melanogaster larval development and immunity. Genetics 2011, 187:1067-1075.
    • (2011) Genetics , vol.187 , pp. 1067-1075
    • Walker, J.1    Kwon, S.Y.2    Badenhorst, P.3    East, P.4    McNeill, H.5    Svejstrup, J.Q.6
  • 26
    • 0032541670 scopus 로고    scopus 로고
    • IKAP is a scaffold protein of the IkappaB kinase complex
    • Cohen L., Henzel W.J., Baeuerle P.A. IKAP is a scaffold protein of the IkappaB kinase complex. Nature 1998, 395:292-296.
    • (1998) Nature , vol.395 , pp. 292-296
    • Cohen, L.1    Henzel, W.J.2    Baeuerle, P.A.3
  • 28
    • 0016216828 scopus 로고
    • Familial dysautonomia: diagnosis, pathogenesis and management
    • Axelrod F.B., Nachtigal R., Dancis J. Familial dysautonomia: diagnosis, pathogenesis and management. Adv Pediatr 1974, 21:75-96.
    • (1974) Adv Pediatr , vol.21 , pp. 75-96
    • Axelrod, F.B.1    Nachtigal, R.2    Dancis, J.3
  • 30
    • 59249093238 scopus 로고    scopus 로고
    • Loss of mouse Ikbkap, a subunit of Elongator, leads to transcriptional deficits and embryonic lethality that can be rescued by human IKBKAP
    • Chen Y.T., Hims M.M., Shetty R.S., Mull J., Liu L., Leyne M., Slaugenhaupt S.A. Loss of mouse Ikbkap, a subunit of Elongator, leads to transcriptional deficits and embryonic lethality that can be rescued by human IKBKAP. Mol Cell Biol 2009, 29:736-744.
    • (2009) Mol Cell Biol , vol.29 , pp. 736-744
    • Chen, Y.T.1    Hims, M.M.2    Shetty, R.S.3    Mull, J.4    Liu, L.5    Leyne, M.6    Slaugenhaupt, S.A.7
  • 32
    • 77954310096 scopus 로고    scopus 로고
    • Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats
    • Lee C., Goldberg J. Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats. Cell 2010, 142:123-132.
    • (2010) Cell , vol.142 , pp. 123-132
    • Lee, C.1    Goldberg, J.2
  • 33
    • 0037200023 scopus 로고    scopus 로고
    • A novel specific role for I kappa B kinase complex-associated protein in cytosolic stress signaling
    • Holmberg C., Katz S., Lerdrup M., Herdegen T., Jaattela M., Aronheim A., Kallunki T. A novel specific role for I kappa B kinase complex-associated protein in cytosolic stress signaling. J Biol Chem 2002, 277:31918-31928.
    • (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
  • 35
    • 70350179460 scopus 로고    scopus 로고
    • Elongator function depends on antagonistic regulation by casein kinase Hrr25 and protein phosphatase Sit4
    • Mehlgarten C., Jablonowski D., Breunig K.D., Stark M.J., Schaffrath R. Elongator function depends on antagonistic regulation by casein kinase Hrr25 and protein phosphatase Sit4. Mol Microbiol 2009, 73:869-881.
    • (2009) Mol Microbiol , vol.73 , pp. 869-881
    • Mehlgarten, C.1    Jablonowski, D.2    Breunig, K.D.3    Stark, M.J.4    Schaffrath, R.5
  • 37
    • 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., Schaffrath R. Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 2003, 49:1297-1307.
    • (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
  • 39
    • 0034724683 scopus 로고    scopus 로고
    • The Elp2 subunit of Elongator and elongating RNA polymerase II holoenzyme is a WD40 repeat protein
    • Fellows J., Erdjument-Bromage H., Tempst P., Svejstrup J.Q. The Elp2 subunit of Elongator and elongating RNA polymerase II holoenzyme is a WD40 repeat protein. J Biol Chem 2000, 275:12896-12899.
    • (2000) J Biol Chem , vol.275 , pp. 12896-12899
    • Fellows, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Svejstrup, J.Q.4
  • 40
    • 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., Svejstrup J.Q. Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator. J Biol Chem 2004, 279:32087-32092.
    • (2004) J Biol Chem , vol.279 , pp. 32087-32092
    • Petrakis, T.G.1    Wittschieben, B.O.2    Svejstrup, J.Q.3
  • 41
    • 0034730176 scopus 로고    scopus 로고
    • A Stat3-interacting protein (StlP1) regulates cytokine signal transduction
    • Collum R.G., Brutsaert S., Lee G., Schindler C. A Stat3-interacting protein (StlP1) regulates cytokine signal transduction. Proc Natl Acad Sci U S A 2000, 97:10120-10125.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10120-10125
    • Collum, R.G.1    Brutsaert, S.2    Lee, G.3    Schindler, C.4
  • 42
    • 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., Onesti S. The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine. Mol Microbiol 2006, 59:795-806.
    • (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
  • 43
    • 58649104923 scopus 로고    scopus 로고
    • An iron-sulfur cluster domain in Elp3 important for the structural integrity of Elongator
    • Greenwood C., Selth L.A., Dirac-Svejstrup A.B., Svejstrup J.Q. An iron-sulfur cluster domain in Elp3 important for the structural integrity of Elongator. J Biol Chem 2009, 284:141-149.
    • (2009) J Biol Chem , vol.284 , pp. 141-149
    • Greenwood, C.1    Selth, L.A.2    Dirac-Svejstrup, A.B.3    Svejstrup, J.Q.4
  • 45
    • 0035902781 scopus 로고    scopus 로고
    • Structure of histone acetyltransferases
    • Marmorstein R. Structure of histone acetyltransferases. J Mol Biol 2001, 311:433-444.
    • (2001) J Mol Biol , vol.311 , pp. 433-444
    • Marmorstein, R.1
  • 48
    • 0037022226 scopus 로고    scopus 로고
    • Human Elongator facilitates RNA polymerase II transcription through chromatin
    • Kim J.H., Lane W.S., Reinberg D. Human Elongator facilitates RNA polymerase II transcription through chromatin. Proc Natl Acad Sci U S A 2002, 99:1241-1246.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1241-1246
    • Kim, J.H.1    Lane, W.S.2    Reinberg, D.3
  • 49
    • 79953086676 scopus 로고    scopus 로고
    • The nuts and bolts of ring-translocase structure and mechanism
    • Lyubimov A.Y., Strycharska M., Berger J.M. The nuts and bolts of ring-translocase structure and mechanism. Curr Opin Struct Biol 2011, 21:240-248.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 240-248
    • Lyubimov, A.Y.1    Strycharska, M.2    Berger, J.M.3
  • 51
    • 0027980497 scopus 로고
    • Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest induced by Kluyveromyces lactis toxin
    • Butler A.R., White J.H., Folawiyo Y., Edlin A., Gardiner D., Stark M.J. Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest induced by Kluyveromyces lactis toxin. Mol Cell Biol 1994, 14:6306-6316.
    • (1994) Mol Cell Biol , vol.14 , pp. 6306-6316
    • Butler, A.R.1    White, J.H.2    Folawiyo, Y.3    Edlin, A.4    Gardiner, D.5    Stark, M.J.6
  • 53
    • 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., Schaffrath R. Molecular analysis of KTI12/TOT4, a Saccharomyces cerevisiae gene required for Kluyveromyces lactis zymocin action. Mol Microbiol 2002, 43:783-791.
    • (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
  • 54
    • 49349093245 scopus 로고    scopus 로고
    • A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3
    • Bar C., Zabel R., Liu S., Stark M.J., Schaffrath R. A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3. Mol Microbiol 2008, 69:1221-1233.
    • (2008) Mol Microbiol , vol.69 , pp. 1221-1233
    • Bar, C.1    Zabel, R.2    Liu, S.3    Stark, M.J.4    Schaffrath, R.5
  • 55
    • 20044367838 scopus 로고    scopus 로고
    • The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast
    • Li F., Lu J., Han Q.J., Zhang G.P., Huang B.Q. The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast. Mol Genet Genomics 2005, 273:264-272.
    • (2005) Mol Genet Genomics , vol.273 , pp. 264-272
    • Li, F.1    Lu, J.2    Han, Q.J.3    Zhang, G.P.4    Huang, B.Q.5
  • 56
    • 84871490369 scopus 로고    scopus 로고
    • A coordinated codon-dependent regulation of translation by Elongator
    • Bauer F., Hermand D. A coordinated codon-dependent regulation of translation by Elongator. Cell Cycle 2012, 11.
    • (2012) Cell Cycle , pp. 11
    • Bauer, F.1    Hermand, D.2
  • 57
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley L.A., Sternberg M.J. Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 2009, 4:363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.