Tethering Creates Unusual Kinetics for Ribosome-Associated Chaperones with Nascent Chains

被引：3

作者：

Witt, Stephan N. ^{[1
]}

机构：

[1] Louisiana State Univ, Hlth Sci Ctr, Dept Biochem & Mol Biol, Shreveport, LA 71130 USA

来源：

PROTEIN AND PEPTIDE LETTERS | 2009年 / 16卷 / 06期

关键词：

Chaperone; holdase; kinetic partitioning; proximity effect; ribosome-associated chaperone; NEWLY SYNTHESIZED PROTEINS; MOLECULAR CHAPERONES; ESCHERICHIA-COLI; TRIGGER FACTOR; SECB; DNAK; BINDING; COMPLEX;

D O I：

10.2174/092986609788490195

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This article focuses on ribosome-associated chaperones. A chaperone bound close to the exit tunnel on a ribosome 25 angstrom from the emerging nascent chain has an effective concentration of 1 x 10(-1) M, which is 4-5 orders of magnitude larger than the concentration of the chaperone in the cytosol. Ribosome-bound chaperones bind nascent chains intramolecularly with rates as large as 10(4) s(-1) in order to keep chains unfolded.

引用

页码：631 / 634

页数：4

共 27 条

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[4] The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb
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