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Cited by 369

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Snf1--a Histone Kinase That Works in Concert with the Histone Acetyltransferase Gcn5 to Regulate Transcription

Lo, Wan-Sheng, Duggan, Laura, Tolga, N. C., Emre, Belotserkovskya, Rimma, Lane, William S., Shiekhattar, Ramin, Berger, Shelley L.·2001·Science

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.

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Metadata

Authors
Lo, W.-S., Duggan, L., Tolga, N. C., Emre, Belotserkovskya, R., Lane, W. S., Shiekhattar, R., & Berger, S. L.
Venue
Science
Published
2001-08-10
Volume
293
Issue
5532
Pages
1142-1146
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2069428708
Cited by
369
References
2
FWCI
11.40
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Snf1--a Histone Kinase That Works in Concert with the Histone Acetyltransferase Gcn5 to Regulate Transcription. https://app.cochat.ai/papers/10.1126/science.1062322
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Lo, W.-S., Duggan, L., Tolga, N. C., Emre, 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. https://doi.org/10.1126/science.1062322

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