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酿酒酵母中与URS1转录抑制位点结合的异源三聚体蛋白的纯化。

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

作者信息

Luche R M, Smart W C, Cooper T G

机构信息

Department of Microbiology and Immunology, University of Tennessee, Memphis 38163.

出版信息

Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7412-6. doi: 10.1073/pnas.89.16.7412.

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.

摘要

与酿酒酵母中许多基因上游的URS1位点结合的蛋白质是该生物体转录全局负调控的核心元件。受该蛋白质调控表达的基因包括参与氮代谢、碳代谢、电子传递、肌醇代谢、热休克反应、减数分裂和孢子形成的基因。这种结合URS1因子(BUF)已被纯化,并且显示为一种由37.5 kDa和73.5 kDa单体组成的异源蛋白质。BUF的异源形式在溶液中以及与其DNA靶位点结合时都能稳定维持。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16be/49720/d671f31f9708/pnas01090-0136-a.jpg

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