Affiliation:
1. Department of Pharmacology, School of Medicine, University of Washington, Seattle, Washington 98195-7280
Abstract
ABSTRACT
The TATA-binding protein (TBP)-associated factor TAF
II
250 is the largest component of the basal transcription factor IID (TFIID). A missense mutation that maps to the acetyltransferase domain of TAF
II
250 induces the temperature-sensitive (
ts
) mutant hamster cell lines ts13 and tsBN462 to arrest in late G
1
. At the nonpermissive temperature (39.5°C), transcription from only a subset of protein encoding genes, including the G
1
cyclins, is dramatically reduced in the mutant cells. Here we demonstrate that the ability of the
ts13
allele of TAF
II
250 to acetylate histones in vitro is temperature sensitive suggesting that this enzymatic activity is compromised at 39.5°C in the mutant cells. Mutagenesis of a putative acetyl coenzyme A binding site produced a TAF
II
250 protein that displayed significantly reduced histone acetyltransferase activity but retained TBP and TAF
II
150 binding. Expression of this mutant in ts13 cells was unable to complement the cell cycle arrest or transcriptional defect observed at 39.5°C. These data suggest that TAF
II
250 acetyltransferase activity is required for cell cycle progression and regulates the expression of essential proliferative control genes.
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
Cited by
62 articles.
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