Document Detail


Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import.
MedLine Citation:
PMID:  17376159     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In Arabidopsis, Hsp93 is encoded by two genes, atHSP93-V and atHSP93-III. We identified two T-DNA mutants for atHSP93-III: one being a partial 'knockdown' (hsp93-III-1) and the other a complete 'knockout' (hsp93-III-2). Homozygotes for both mutants were indistinguishable from wild type. We crossed each mutant to an atHSP93-V knockout, and identified double mutants with strongly chlorotic phenotypes. This implied redundancy, which was confirmed by the complementation of mildly chlorotic hsp93-V plants by atHSP93-III over-expression. While the hsp93-V hsp93-III-1 mutant was doubly homozygous, the second double mutant was heterozygous for hsp93-III-2 (genotype: hsp93-V/hsp93-V; +/hsp93-III-2). Attempts to identify an hsp93-V hsp93-III-2 double homozygote were unsuccessful, indicating that the Hsp93 pool is essential for viability. Consistently, siliques of the second double mutant contained aborted seeds (because of a block in the zygote-embryo transition) and failed ovules (because of a moderate defect in female gametophytes). Double-mutant plants were chlorophyll-deficient, contained under-developed chloroplasts, and exhibited stunted growth. In import assays using a chimeric pre-protein (plastocyanin transit peptide fused to dihydrofolate reductase; PC-DHFR), a clear defect was observed in hsp93-V hsp93-III-1 chloroplasts. Interestingly, while denaturation or stabilization of the DHFR moiety had a strong effect on import efficiency in the wild type, no such effects were observed with double-mutant (or tic40) chloroplasts. This indicated that pre-protein unfolding is not rate-limiting for import into mutant chloroplasts, and suggested that (unlike the situation in mitochondria) the inner membrane import machinery does not contribute to pre-protein unfolding at the organellar surface.
Authors:
Sabina Kovacheva; Jocelyn Bédard; Anthony Wardle; Ramesh Patel; Paul Jarvis
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-03-21
Journal Detail:
Title:  The Plant journal : for cell and molecular biology     Volume:  50     ISSN:  0960-7412     ISO Abbreviation:  Plant J.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-04-20     Completed Date:  2007-08-13     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9207397     Medline TA:  Plant J     Country:  England    
Other Details:
Languages:  eng     Pagination:  364-79     Citation Subset:  IM    
Affiliation:
Department of Biology, University of Leicester, Leicester LE1 7RH, UK.
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MeSH Terms
Descriptor/Qualifier:
Animals
Arabidopsis Proteins / genetics,  physiology*
Chlorophyll / metabolism
Chloroplasts / metabolism,  ultrastructure
Heat-Shock Proteins / genetics,  physiology*
Immunoblotting
Mice
Microscopy, Electron, Transmission
Molecular Chaperones / genetics,  physiology*
Mutation
Phenotype
Plants, Genetically Modified
Plastids / metabolism*
Protein Transport / genetics,  physiology
Recombinant Fusion Proteins / genetics,  metabolism
Reverse Transcriptase Polymerase Chain Reaction
Seeds / cytology,  genetics,  metabolism
Tetrahydrofolate Dehydrogenase / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Heat-Shock Proteins; 0/Molecular Chaperones; 0/Recombinant Fusion Proteins; 1406-65-1/Chlorophyll; EC 1.5.1.3/Tetrahydrofolate Dehydrogenase

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