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The mitochondrial hsp70 chaperone system : effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70

Azem, A. and Oppliger, W. and Lustig, A. and Jeno, P. and Feifel, B. and Schatz, G. and Horst, M.. (1997) The mitochondrial hsp70 chaperone system : effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70. Journal of Biological Chemistry, Vol. 272, H. 33. pp. 20901-20906.

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Official URL: http://edoc.unibas.ch/dok/A5258319

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Abstract

Mitochondrial hsp70 (mhsp70) is a key component in the import and folding of mitochondrial proteins. In both processes, mhsp70 cooperates with the mitochondrial nucleotide exchange factor mGrpE (also termed Mge1p). In this work we have characterized the self-association of purified mhsp70, the interaction of mhsp70 with isolated mGrpE and protein substrate, and the effect of nucleotides on these interactions. mhsp70 can form oligomers that are dissociated by ATP or by a nonhydrolyzable ATP analog. A substrate peptide binds to mhsp70 in the absence of added nucleotides and is released by ATP but not by ADP. Binding of the peptide causes nucleotide-independent dissociation of the mhsp70 oligomers and enhances the mhsp70 ATPase. Purified mGrpE forms a homodimer. In the absence of added nucleotides, one mGrpE dimer binds to one molecule of mhsp70, forming a stable 122 kDa hetero-oligomer. This complex is weakened by ADP and completely dissociated by ATP.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Services Biozentrum > Mass Spectrometry (Jenö)
UniBasel Contributors:Jenö, Paul
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society of Biological Chemists
ISSN:0021-9258
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:20

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