Document Detail


The prosequence of pro-sigmaK promotes membrane association and inhibits RNA polymerase core binding.
MedLine Citation:
PMID:  9573196     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Pro-sigmaK is the inactive precursor of sigmaK, a mother cell-specific sigma factor responsible for the transcription of late sporulation genes of Bacillus subtilis. Upon subcellular fractionation, the majority of the pro-sigmaK was present in the membrane fraction. The rest of the pro-sigmaK was in a large complex that did not contain RNA polymerase core subunits. In contrast, the majority of the sigmaK was associated with core RNA polymerase. Virtually identical fractionation properties were observed when pro-sigmaE was analyzed. Pro-sigmaK was completely solubilized from the membrane fraction and the large complex by Triton X-100 and was partially solubilized from the membrane fraction by NaCl and KSCN. The membrane association of pro-sigmaK did not require spoIVF gene products, which appear to be located in the mother cell membrane that surrounds the forespore, and govern pro-sigmaK processing in the mother cell. Furthermore, pro-sigmaK associated with the membrane when overproduced in vegetative cells. Overproduction of pro-sigmaK in sporulating cells resulted in more pro-sigmaK in the membrane fraction. In agreement with the results of cell fractionation experiments, immunofluorescence microscopy showed that pro-sigmaK was localized to the mother cell membranes that surround the mother cell and the forespore in sporulating wild-type cells and mutant cells that do not process pro-sigmaK. Treatment of extracts with 0.6 M KCl appeared to free most of the pro-sigmaK and sigmaK from other cell constituents. After salt removal, sigmaK, but not pro-sigmaK, reassociated with exogenous core RNA polymerase to form holoenzyme. These results suggest that the prosequence inhibits RNA polymerase core binding and targets pro-sigmaK to the membrane, where it may interact with the processing machinery.
Authors:
B Zhang; A Hofmeister; L Kroos
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of bacteriology     Volume:  180     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  1998 May 
Date Detail:
Created Date:  1998-06-01     Completed Date:  1998-06-01     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2434-41     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Michigan State University, East Lansing 48824, USA.
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MeSH Terms
Descriptor/Qualifier:
Bacillus subtilis / physiology*
Bacterial Proteins
Cell Compartmentation
Cell Fractionation
DNA-Directed RNA Polymerases / metabolism*
Fluorescent Antibody Technique
Membrane Proteins / metabolism*
Membranes / drug effects
Models, Biological
Octoxynol / pharmacology
Protein Binding
Protein Processing, Post-Translational
Protein Sorting Signals / metabolism*
Sigma Factor / metabolism*
Signal Transduction
Spores, Bacterial / physiology
Transcription Factors / metabolism*
Grant Support
ID/Acronym/Agency:
GM18568/GM/NIGMS NIH HHS; GM43585/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Membrane Proteins; 0/Protein Sorting Signals; 0/Sigma Factor; 0/Transcription Factors; 0/pro-sigmaK protein, Bacillus subtilis; 0/sigma K; 9002-93-1/Octoxynol; EC 2.7.7.6/DNA-Directed RNA Polymerases
Comments/Corrections

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


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