PURIFICATION OF THE HETEROMERIC PROTEIN-BINDING TO THE URS1 TRANSCRIPTIONAL REPRESSION SITE IN SACCHAROMYCES-CEREVISIAE

被引:41
作者
LUCHE, RM
SMART, WC
COOPER, TG
机构
[1] Microbiology/Immunology Department, University of Tennessee, Memphis
关键词
D O I
10.1073/pnas.89.16.7412
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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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页码:7412 / 7416
页数:5
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