Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin- mediated protein folding Journal Article

  

Authors:	Hlodan, R.; Tempst, P.; Hartl, F. U.
Article Title:	Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin- mediated protein folding
Abstract:	Unfolded rhodanese in a complex with the chaperonin GroEL was subjected to limited proteolysis. Sequence analysis indentified a GroEL-bound fragment of -11,000 Mr and a well defined fragment of -7,000 Mr from the two homologous domains of rhodanese. The shorter segment contains one hydrophobic and one amphiphilic α-helix mapping to the domain interface while the other fragment contains the homologous regions and an additional hydrophobic helix. Our results suggest a mechanism for the GroEL-mediated folding of rhodanese in which the domain-forming regions of the polypeptide are kept apart and are then released, perhaps sequentially, resulting in correct folding. © 1995 Nature Publishing Group.
Keywords:	animal; protein degradation; protein binding; amino acid sequence; molecular sequence data; peptide fragments; models, molecular; protein structure, tertiary; cattle; proteinase; protein folding; sequence homology; protein structure, secondary; in vitro; peptide mapping; polypeptide; hydrophobicity; chaperonins; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; macromolecular systems; chaperonin; groel protein; thiosulfate sulfurtransferase
Journal Title:	Nature Structural Biology
Volume:	2
Issue:	7
ISSN:	1072-8368
Publisher:	Nature Publishing Group
Date Published:	1995-07-01
Start Page:	587
End Page:	595
Language:	English
DOI:	10.1038/nsb0795-587
PUBMED:	7664127
PROVIDER:	scopus
DOI/URL:	https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029127242&doi=10.1038%2fnsb0795-587&partnerID=40&md5=fb8d212836331bfa09899c92f8f4b457
Notes:	Article -- Export Date: 28 August 2018 -- Source: Scopus

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