A multiprotein complex that interacts with RNA polymerase II elongator Journal Article


Authors: Li, Y.; Takagi, Y.; Jiang, Y.; Tokunaga, M.; Erdjument-Bromage, H.; Tempst, P.; Kornberg, R. D.
Article Title: A multiprotein complex that interacts with RNA polymerase II elongator
Abstract: A three-subunit Hap complex that interacts with the RNA polymerase II Elongator was isolated from yeast. Deletions of genes for two Hap subunits, HAP1 and HAP3, confer pGKL killer-insensitive and weak Elongator phenotypes. Preferential interaction of the Hap complex with free rather than RNA polymerase II-associated Elongator suggests a role in the regulation of Elongator activity.
Keywords: unclassified drug; gene deletion; genetics; mutation; nonhuman; molecular genetics; proteins; phenotype; genes; biological model; models, biological; protein protein interaction; protein binding; gene product; transcription factor; enzymology; phosphorylation; transcription factors; rna; chemistry; amino acid sequence; molecular sequence data; sequence homology, amino acid; saccharomyces cerevisiae; nucleotide sequence; serodiagnosis; yeast; saccharomyces cerevisiae proteins; protein subunit; saccharomyces cerevisiae protein; enzyme kinetics; sequence homology; biochemistry; isolation and purification; rna polymerase ii; lyase; fungal protein; polyacrylamide gel electrophoresis; electrophoresis, polyacrylamide gel; elongation factor; fungal proteins; protein hap1; histone acetyltransferase; phenotypes; enzyme isolation; precipitin tests; priority journal; article; carbon-oxygen lyases; dna-(apurinic or apyrimidinic site) lyase; elongator protein; protein hap3; ccaat binding factor; dna (apurinic or apyrimidinic site) lyase; hap3 protein, s cerevisiae; hap3 transcription factor protein, fungal; ccaat-binding factor
Journal Title: Journal of Biological Chemistry
Volume: 276
Issue: 32
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 2001-08-10
Start Page: 29628
End Page: 29631
Language: English
DOI: 10.1074/jbc.C100274200
PUBMED: 11390369
PROVIDER: scopus
DOI/URL:
Notes: Export Date: 21 May 2015 -- Source: Scopus
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  1. Paul J Tempst
    324 Tempst