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    
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.
Chun-Song Chua; Huiyu Low; Kian-Sim Goo; T S Sim
Related Documents :
24223527 - Quantification of drive-response relationships between residues during protein folding.
19645507 - On the mechanism of nonspecific inhibitors of protein aggregation: dissecting the inter...
15651637 - Compatible and counteracting solutes: protecting cells from the dead sea to the deep sea.
15280037 - Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates.
19682997 - Effect of macromolecular crowding on protein folding dynamics at the secondary structur...
22730767 - Proteomic differences in seed filling between yellow-seeded progeny of brassica napus-s...
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    
Department of Microbiology, Yong Loo Lin School of Medicine, National University of Singapore, 5 Science Drive 2, Singapore, 117597, Singapore.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Adenosine Triphosphatases / antagonists & inhibitors
Adenosine Triphosphate / pharmacology
Amino Acid Sequence
Amino Acids
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
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

Previous Document:  Cryopyrin-associated periodic syndromes: background and therapeutics.
Next Document:  The impact on microtubule network of a bracovirus IkappaB-like protein.