A multiprotein complex that interacts with RNA polymerase II elongator.
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.
Li
Y
Y
Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5400, USA. yli@tularik.com
Takagi
Y
Y
Jiang
Y
Y
Tokunaga
M
M
Erdjument-Bromage
H
H
Tempst
P
P
Kornberg
R D
RD
D000595:Amino Acid Sequence; D023081:CCAAT-Binding Factor / Q000235:genetics; D019757:Carbon-Oxygen Lyases / Q000235:genetics; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000235:genetics; D008954:Models, Biological; D008969:Molecular Sequence Data; D009154:Mutation; D010641:Phenotype; D010766:Phosphorylation; D011233:Precipitin Tests; D011485:Protein Binding; D012319:RNA Polymerase II / Q000737:chemistry* / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000235:genetics
D023081:CCAAT-Binding Factor; D005656:Fungal Proteins; C490431:HAP3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D012319:RNA Polymerase II; D019757:Carbon-Oxygen Lyases; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase