Purification of the heteromeric protein binding to the URS1 transcriptional repression site in Saccharomyces cerevisiae

R. M. Luche, W. C. Smart, Terrance Cooper

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32 Citations (Scopus)

Abstract

The protein that binds to the URS1 site situated upstream of many genes in Saccharomyces cerevisiae is a central element responsible for global negative control of transcription in this organism. Among the genes whose expression is regulated by this protein are those that participate in nitrogen metabolism, carbon metabolism, electron transport, inositol metabolism, heat shock response, meiosis, and sporulation. This factor, binding URS1 factor (BUF), has been purified and shown to be a heteromeric protein composed of 37.5- and 73.5-kDa monomers. The heteromeric form of BUF is stably maintained both in solution and bound to its DNA target site.

Original languageEnglish (US)
Pages (from-to)7412-7416
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number16
DOIs
StatePublished - Jan 1 1992

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Protein Binding
Saccharomyces cerevisiae
Heat-Shock Response
Proteins
Meiosis
Inositol
Electron Transport
Nitrogen
Carbon
Gene Expression
DNA
Genes

All Science Journal Classification (ASJC) codes

  • General

Cite this

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AB - The protein that binds to the URS1 site situated upstream of many genes in Saccharomyces cerevisiae is a central element responsible for global negative control of transcription in this organism. Among the genes whose expression is regulated by this protein are those that participate in nitrogen metabolism, carbon metabolism, electron transport, inositol metabolism, heat shock response, meiosis, and sporulation. This factor, binding URS1 factor (BUF), has been purified and shown to be a heteromeric protein composed of 37.5- and 73.5-kDa monomers. The heteromeric form of BUF is stably maintained both in solution and bound to its DNA target site.

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