Document Detail


Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein response.
MedLine Citation:
PMID:  23290031     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
PspA, -B and -C regulate the bacterial phage shock protein stress response by controlling the PspF transcription factor. Here, we have developed complementary approaches to study the behaviour of these proteins at their endogenous levels in Yersinia enterocolitica. First, we observed GFP-tagged versions with an approach that resolves individual protein complexes in live cells. This revealed that PspA, -B and -C share common behaviours, including a striking contrast before and after induction. In uninduced cells, PspA, -B and -C were highly mobile and widely distributed. However, induction reduced mobility and the proteins became more organized. Combining mCherry- and GFP-tagged proteins also revealed that PspA colocalizes with PspB and PspC into large stationary foci, often located close to the pole of induced cells. In addition, co-immunoprecipitation assays provided the first direct evidence supporting the model that PspA switches binding partners from PspF to PspBC upon induction. Together, these data suggest that PspA, -B and -C do not stably interact and are highly mobile before induction, perhaps sampling the status of the membrane and each other. However, an inducing signal promotes PspABC complex formation and their relocation to discrete parts of the membrane, which might then be important for mitigating envelope stress.
Authors:
Saori Yamaguchi; Dylan A Reid; Eli Rothenberg; Andrew J Darwin
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2013-01-07
Journal Detail:
Title:  Molecular microbiology     Volume:  87     ISSN:  1365-2958     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-25     Completed Date:  2013-07-05     Revised Date:  2014-02-04    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  656-71     Citation Subset:  IM    
Copyright Information:
© 2013 Blackwell Publishing Ltd.
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MeSH Terms
Descriptor/Qualifier:
Artificial Gene Fusion
Bacterial Proteins / metabolism*
Cell Membrane / chemistry
Gene Expression Regulation, Bacterial*
Genes, Reporter
Heat-Shock Proteins / metabolism*
Immunoprecipitation
Luminescent Proteins / analysis,  genetics
Protein Binding
Protein Interaction Mapping
Recombinant Fusion Proteins
Staining and Labeling
Stress, Physiological*
Yersinia enterocolitica / physiology*
Grant Support
ID/Acronym/Agency:
R01 AI052148/AI/NIAID NIH HHS; R01AI052148/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Heat-Shock Proteins; 0/Luminescent Proteins; 0/Recombinant Fusion Proteins; 0/phage shock protein, Bacteria
Comments/Corrections

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