Document Detail


Characterization of Plasmodium falciparum co-chaperone p23: its intrinsic chaperone activity and interaction with Hsp90.
MedLine Citation:
PMID:  20140477     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
It is well known that the co-chaperone p23 regulates Hsp90 chaperone activity in protein folding. In Plasmodium falciparum, a putative p23 (Pfp23) has been identified through genome analysis, but its authenticity has remained unconfirmed since co-immunoprecipitation experiments failed to show its interaction with P. falciparum Hsp90 (PfHsp90). Thus, recombinant Pfp23 and PfHsp90 proteins purified from expressed clones were used in this study. It was clear that Pfp23 exhibited chaperone activity by virtue of its ability to suppress citrate synthase aggregation at 45 degrees C. Pfp23 was also shown to interact with PfHsp90 and to suppress its ATPase activity. Analyses of modeled Pfp23-PfHsp90 protein complex and site-directed mutagenesis further revealed strategically placed amino acid residues, K91, H93, W94 and K96, in Pfp23 to be crucial for binding PfHsp90. Collectively, this study has provided experimental evidence for the inherent chaperone function of Pfp23 and its interaction with PfHsp90, a sequel widely required for client protein activation.
Authors:
Chun-Song Chua; Huiyu Low; Kian-Sim Goo; T S Sim
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Publication Detail:
Type:  Journal Article     Date:  2010-02-06
Journal Detail:
Title:  Cellular and molecular life sciences : CMLS     Volume:  67     ISSN:  1420-9071     ISO Abbreviation:  Cell. Mol. Life Sci.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-04-23     Completed Date:  2010-05-05     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9705402     Medline TA:  Cell Mol Life Sci     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  1675-86     Citation Subset:  IM    
Affiliation:
Department of Microbiology, Yong Loo Lin School of Medicine, National University of Singapore, 5 Science Drive 2, Singapore, 117597, Singapore.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / antagonists & inhibitors
Adenosine Triphosphate / pharmacology
Amino Acid Sequence
Amino Acids
Animals
Cloning, Molecular
Computational Biology
Electrophoresis, Polyacrylamide Gel
HSP90 Heat-Shock Proteins / metabolism*
Magnesium Chloride / pharmacology
Models, Molecular
Molecular Chaperones / metabolism*
Molecular Sequence Data
Mutant Proteins / metabolism
Plasmodium falciparum / drug effects,  metabolism*
Protein Binding / drug effects
Protozoan Proteins / chemistry,  metabolism*
Recombinant Proteins / metabolism
Repetitive Sequences, Amino Acid
Sequence Deletion
Structure-Activity Relationship
Chemical
Reg. No./Substance:
0/Amino Acids; 0/HSP90 Heat-Shock Proteins; 0/Molecular Chaperones; 0/Mutant Proteins; 0/Protozoan Proteins; 0/Recombinant Proteins; 56-65-5/Adenosine Triphosphate; 7786-30-3/Magnesium Chloride; EC 3.6.1.-/Adenosine Triphosphatases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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