Minimal machinery of RNA polymerase holoenzyme sufficient for promoter melting

被引：67

作者：

Young, BA

Gruber, TM

Gross, CA ^{[1
]}

机构：

[1] Univ Calif San Francisco, Dept Stomatol, San Francisco, CA 94143 USA

[2] Univ Calif San Francisco, Dept Microbiol & Immunol, San Francisco, CA 94143 USA

来源：

SCIENCE | 2004年 / 303卷 / 5662期

关键词：

D O I：

10.1126/science.1092462

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：

We determined the minimal portion of Escherichia coli RNA polymerase ( RNAP) holoenzyme able to accomplish promoter melting, the crucial step in transcription initiation that provides RNAP access to the template strand. Upon duplex DNA binding, the N terminus of the beta' subunit ( amino acids 1 to 314) and amino acids 94 to 507 of the sigma subunit, together comprising less than one-fifth of RNAP holoenzyme, were able to melt an extended - 10 promoter in a reaction remarkably similar to that of authentic holoenzyme. Our results support the model that capture of nontemplate bases extruded from the DNA helix underlies the melting process.

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页码：1382 / 1384

页数：3

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