In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System
Abstract
The quantitative contribution of chaperonin GroEL to protein folding in E. coli was analyzed. A diverse set of newly synthesized polypeptides, predominantly between 10–55 kDa, interacts with GroEL, accounting for 10%–15% of all cytoplasmic protein under normal growth conditions, and for 30% or more upon exposure to heat stress. Most proteins leave GroEL rapidly within 10–30 s. We distinguish three classes of substrate proteins: (I) proteins with...
Paper Details
Title
In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System
Published Date
Aug 1, 1997
Journal
Volume
90
Issue
3
Pages
491 - 500
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