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

被引:395
作者
Wittschieben, BO
Otero, G
de Bizemont, T
Fellows, J
Erdjument-Bromage, H
Ohba, R
Li, Y
Allis, CD
Tempst, P
Svejstrup, JQ
机构
[1] Imperial Canc Res Fund, Clare Hall Labs, S Mimms EN6 3LD, Herts, England
[2] Mem Sloan Kettering Canc Ctr, Program Mol Biol, New York, NY 10021 USA
[3] Univ Virginia, Hlth Sci Ctr, Dept Mol Genet & Biochem, Charlottesville, VA 22908 USA
[4] Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA
关键词
D O I
10.1016/S1097-2765(00)80194-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 role for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.
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页码:123 / 128
页数:6
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