Publication Date:
1995-08-11
Description:
The Escherichia coli chaperonin GroEL and its regulator GroES are thought to mediate adenosine triphosphate-dependent protein folding as an asymmetrical complex, with substrate protein bound within the GroEL cylinder. In contrast, a symmetrical complex formed between one GroEL and two GroES oligomers, with substrate protein binding to the outer surface of GroEL, was recently proposed to be the functional chaperonin unit. Electron microscopic and biochemical analyses have now shown that unphysiologically high magnesium concentrations and increased pH are required to assemble symmetrical complexes, the formation of which precludes the association of unfolded polypeptide. Thus, the functional significance of GroEL:(GroES)2 particles remains to be demonstrated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engel, A -- Hayer-Hartl, M K -- Goldie, K N -- Pfeifer, G -- Hegerl, R -- Muller, S -- da Silva, A C -- Baumeister, W -- Hartl, F U -- GM 50908/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):832-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Maurice E. Muller Institute, Biozentrum, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638600" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphate/pharmacology
;
Adenylyl Imidodiphosphate/pharmacology
;
Chaperonin 10/chemistry/*metabolism/ultrastructure
;
Chaperonin 60/chemistry/*metabolism/ultrastructure
;
Hydrogen-Ion Concentration
;
Magnesium/pharmacology
;
Microscopy, Electron, Scanning Transmission
;
Protein Folding
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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