Title: Determination of Chaperonin Activity In Vivo
Abstract: AbstractDuring the last 10 years, much effort has been made to unravel the molecular mechanism by which the chaperonins, in particular GroEL and GroES proteins from Escherichia coli (E. coli), facilitate the correct folding of a variety of unrelated polypeptides. Most of these studies have been carried out using purified proteins for in vitro analysis. Although we have learned a great deal about the remarkable manner by which the E. coli chaperonin machine facilitates polypeptide folding (reviewed in refs. 1-3), ultimately it is the activity of the chaperonins in their biological context (inside the cell) that is of the most interest. Despite the difficulty of studying these proteins in their natural environment, there are a couple of reports that address this question (4,5). In this chapter, we describe assays that can be used to determine whether or not different chaperonin proteins (either mutant forms of GroEL and GroES or "putative" chaperonins from other organisms) are able to function in E. coli. The advantage of using E. coli for such studies is:KeywordsSoft AgarRecipient StrainPlaque SizeBacterial LawngroEL GeneThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Publication Year: 2003
Publication Date: 2003-11-14
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 2
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