Elongator complex protein 3 (Q02908)

Identification
NameElongator complex protein 3
Synonyms
  • Gamma-toxin target 3
Gene NameELP3
Enzyme Class
Biological Properties
General FunctionInvolved in N-acetyltransferase activity
Specific FunctionActs as catalytic subunit of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. ELP3 is required for the complex integrity and for the association of the complex with nascent RNA transcript. Independently, ELP3 may be involved in polarized exocytosis. Is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA
Cellular LocationCytoplasm. Nucleus
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00045Coenzyme AShow
YMDB00312Acetyl-CoAShow
GO Classification
Component
Not Available
Function
N-acetyltransferase activity
catalytic activity
transferase activity
binding
metal cluster binding
iron-sulfur cluster binding
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
acyltransferase activity
acetyltransferase activity
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 16
LocusYPL086C
Gene Sequence>1674 bp ATGGCTCGTCATGGAAAAGGCCCAAAAACTAACAAAAAAAAGCTAGCACCTGAAAAGGAA AGGTTTATACAATGTTGTGCTGATATCACATTAGAGTTAACAGATTCTTTAACCTCGGGA ACAACAAGAGAAATTAATCTGAATGGTTTGATTACTAAATATTCAAAGAAATATAAACTA AAGCAACAACCAAGGTTAACCGATATCATTAATTCTATTCCAGACCAATACAAAAAATAT TTATTACCCAAATTGAAGGCTAAGCCAGTAAGAACAGCATCGGGTATTGCAGTGGTAGCC GTTATGTGTAAACCACATCGTTGTCCTCACATTGCATATACAGGTAATATTTGTGTTTAT TGTCCAGGTGGTCCAGATTCAGATTTTGAGTATTCTACACAATCTTACACAGGCTATGAA CCAACTTCAATGCGTGCCATCAGAGCTCGTTATGACCCTTATGAACAAGCACGTGGTAGG GTGGAACAATTGAAACAGTTAGGTCACTCCATCGATAAAGTCGAATATGTTCTGATGGGT GGTACATTTATGTCATTACCAAAAGAATATCGTGAAGATTTTATTGTGAAATTGCATAAT GCACTTTCTGGGTTCAATGGTAATGATATTGATGAAGCTATTCTTTATTCGCAACAAAGT TTAACGAAGTGTGTTGGTATAACAATCGAAACTAGGCCTGATTATTGTACGCAAACACAT TTGGACGATATGTTAAAATATGGCTGTACCAGATTAGAAATTGGTGTTCAGTCCTTGTAC GAAGACGTTGCTCGTGATACTAATAGAGGACACACCGTTAGGTCTGTTTGTGAAACTTTT GCTGTGTCTAAAGATGCTGGTTATAAGGTTGTTTCTCACATGATGCCAGATTTACCAAAT GTTGGGATGGAAAGAGATATTGAACAGTTCAAAGAGTATTTTGAAAATCCTGATTTTAGG ACTGATGGGTTGAAAATCTATCCAACTTTAGTCATTAGGGGTACAGGTTTATACGAACTT TGGAAAACGGGCAGGTATAAGTCTTATAGTGCCAACGCCTTAGTGGACTTAGTTGCTAGA ATCTTGGCCCTAGTGCCCCCATGGACAAGAATCTACCGTGTCCAAAGAGACATTCCAATG CCCTTGGTTACCTCAGGTGTTGACAATGGTAACTTGAGAGAATTGGCATTAGCTAGAATG AAGGACTTGGGTACAACTTGTAGGGATGTTCGTACTAGGGAAGTGGGTATCCAAGAAGTG CATCATAAAGTTCAACCAGATCAGGTCGAGCTTATCAGAAGGGATTACTATGCAAATGGT GGTTGGGAAACCTTTTTATCATATGAAGATCCAAAGAAAGATATACTGATTGGTTTGCTG AGATTGAGAAAGGCTTCAAAGAAATATACATATAGAAAAGAATTCACCTCCCAGAGGACT TCTATTGTTAGAGAATTGCATGTTTATGGTTCTGTGGTTCCACTTCATTCAAGAGATCCT CGTAAATTCCAGCATCAAGGGTTTGGTACTCTATTGATGGAAGAAGCGGAAAGAATCGCC AAGGAAGAGCATGGTTCAGAGAAAATTTCTGTTATTTCTGGTGTTGGTGTAAGAAATTAC TATGGTAAACTAGGATATGAACTAGACGGTCCATACATGTCGAAAAGAATTTAA
Protein Properties
Pfam Domain Function
Protein Residues557
Protein Molecular Weight63656.5
Protein Theoretical pI9.28
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Elongator complex protein 3 MARHGKGPKTNKKKLAPEKERFIQCCADITLELTDSLTSGTTREINLNGLITKYSKKYKL KQQPRLTDIINSIPDQYKKYLLPKLKAKPVRTASGIAVVAVMCKPHRCPHIAYTGNICVY CPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYEQARGRVEQLKQLGHSIDKVEYVLMG GTFMSLPKEYREDFIVKLHNALSGFNGNDIDEAILYSQQSLTKCVGITIETRPDYCTQTH LDDMLKYGCTRLEIGVQSLYEDVARDTNRGHTVRSVCETFAVSKDAGYKVVSHMMPDLPN VGMERDIEQFKEYFENPDFRTDGLKIYPTLVIRGTGLYELWKTGRYKSYSANALVDLVAR ILALVPPWTRIYRVQRDIPMPLVTSGVDNGNLRELALARMKDLGTTCRDVRTREVGIQEV HHKVQPDQVELIRRDYYANGGWETFLSYEDPKKDILIGLLRLRKASKKYTYRKEFTSQRT SIVRELHVYGSVVPLHSRDPRKFQHQGFGTLLMEEAERIAKEEHGSEKISVISGVGVRNY YGKLGYELDGPYMSKRI
References
External Links
ResourceLink
Saccharomyces Genome Database ELP3
Uniprot IDQ02908
Uniprot NameELP3_YEAST
GenBank Gene IDU43281
Genebank Protein ID1151240
General Reference
  • Bussey, H., Storms, R. K., Ahmed, A., Albermann, K., Allen, E., Ansorge, W., Araujo, R., Aparicio, A., Barrell, B., Badcock, K., Benes, V., Botstein, D., Bowman, S., Bruckner, M., Carpenter, J., Cherry, J. M., Chung, E., Churcher, C., Coster, F., Davis, K., Davis, R. W., Dietrich, F. S., Delius, H., DiPaolo, T., Hani, J., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Nature 387:103-105.9169875
  • Otero, G., Fellows, J., Li, Y., de Bizemont, T., Dirac, A. M., Gustafsson, C. M., Erdjument-Bromage, H., Tempst, P., Svejstrup, J. Q. (1999). "Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation." Mol Cell 3:109-118.10024884
  • Frohloff, F., Fichtner, L., Jablonowski, D., Breunig, K. D., Schaffrath, R. (2001). "Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin." EMBO J 20:1993-2003.11296232
  • Wittschieben, B. O., Otero, G., de Bizemont, T., Fellows, J., Erdjument-Bromage, H., Ohba, R., Li, Y., Allis, C. D., Tempst, P., Svejstrup, J. Q. (1999). "A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme." Mol Cell 4:123-128.10445034
  • Winkler, G. S., Petrakis, T. G., Ethelberg, S., Tokunaga, M., Erdjument-Bromage, H., Tempst, P., Svejstrup, J. Q. (2001). "RNA polymerase II elongator holoenzyme is composed of two discrete subcomplexes." J Biol Chem 276:32743-32749.11435442
  • Krogan, N. J., Greenblatt, J. F. (2001). "Characterization of a six-subunit holo-elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae." Mol Cell Biol 21:8203-8212.11689709
  • Winkler, G. S., Kristjuhan, A., Erdjument-Bromage, H., Tempst, P., Svejstrup, J. Q. (2002). "Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo." Proc Natl Acad Sci U S A 99:3517-3522.11904415
  • Klassen, R., Meinhardt, F. (2003). "Structural and functional analysis of the killer element pPin1-3 from Pichia inositovora." Mol Genet Genomics 270:190-199.13680368
  • Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S. P. (2003). "A proteomics approach to understanding protein ubiquitination." Nat Biotechnol 21:921-926.12872131
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Petrakis, T. G., Wittschieben, B. O., Svejstrup, J. Q. (2004). "Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-elongator." J Biol Chem 279:32087-32092.15138274
  • Petrakis, T. G., Sogaard, T. M., Erdjument-Bromage, H., Tempst, P., Svejstrup, J. Q. (2005). "Physical and functional interaction between Elongator and the chromatin-associated Kti12 protein." J Biol Chem 280:19454-19460.15772087
  • Rahl, P. B., Chen, C. Z., Collins, R. N. (2005). "Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation." Mol Cell 17:841-853.15780940
  • Huang, B., Johansson, M. J., Bystrom, A. S. (2005). "An early step in wobble uridine tRNA modification requires the Elongator complex." RNA 11:424-436.15769872
  • Paraskevopoulou, C., Fairhurst, S. A., Lowe, D. J., Brick, P., Onesti, S. (2006). "The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine." Mol Microbiol 59:795-806.16420352