A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme Journal Article


Authors: Wittschieben, B. Ø; Otero, G.; De Bizemont, T.; Fellows, J.; Erdjument-Bromage, H.; Ohba, R.; Li, Y.; Allis, C. D.; Tempst, P.; Svejstrup, J. Q.
Article Title: A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme
Abstract: The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histone acetyltransferase (HAT) capable of acetylating core histones in vitro. In vivo, ELP3 gene deletion confers typical elp phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. These results suggest a rote for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.
Keywords: gene deletion; nonhuman; phenotype; cloning, molecular; gene activation; amino acid sequence; molecular sequence data; enzyme analysis; saccharomyces cerevisiae; sequence alignment; chromatin; recombinant proteins; yeast; saccharomyces cerevisiae proteins; enzyme structure; rna polymerase ii; temperature sensitivity; acetyltransferases; fungal proteins; histone acetyltransferase; histone acetyltransferases; article
Journal Title: Molecular Cell
Volume: 4
Issue: 1
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 1999-07-01
Start Page: 123
End Page: 128
Language: English
DOI: 10.1016/s1097-2765(00)80194-x
PUBMED: 10445034
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 16 August 2016 -- Source: Scopus
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  1. Paul J Tempst
    324 Tempst