Snf1 - A histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription

W. S. Lo, L. Duggan, N. C.T. Emre, R. Belotserkovskya, W. S. Lane, R. Shiekhattar, S. L. Berger

Research output: Contribution to journalArticle

280 Scopus citations

Abstract

Modification of histones is an important element in the regulation of gene expression. Previous work suggested a link between acetylation and phosphorylation, but questioned its mechanistic basis. We have purified a histone H3 serine-10 kinase complex from Saccharomyces cerevisiae and have identified its catalytic subunit as Snf1. The Snf1/AMPK family of kinases function in conserved signal transduction pathways. Our results show that Snf1 and the acetyltransferase Gcn5 function in an obligate sequence to enhance INO1 transcription by modifying histone H3 serine-10 and lysine-14. Thus, phosphorylation and acetylation are targeted to the same histone by promoter-specific regulation by a kinase/acetyltransferase pair, supporting models of gene regulation wherein transcription is controlled by coordinated patterns of histone modification.

Original languageEnglish (US)
Pages (from-to)1142-1146
Number of pages5
JournalScience
Volume293
Issue number5532
DOIs
StatePublished - Aug 10 2001
Externally publishedYes

ASJC Scopus subject areas

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    Lo, W. S., Duggan, L., Emre, N. C. T., Belotserkovskya, R., Lane, W. S., Shiekhattar, R., & Berger, S. L. (2001). Snf1 - A histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science, 293(5532), 1142-1146. https://doi.org/10.1126/science.1062322