Document Detail


Protein phosphorylation in Bacillus thuringiensis during growth and delta-endotoxin production.
MedLine Citation:
PMID:  2855529     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
At least 14 phosphopolypeptides in which the phosphate groups were present as mono-esters were detected by pulse labelling of Bacillus thuringiensis subsp. kurstaki HD-1-Dipel with [32P]orthophosphate at different stages of growth and differentiation. Marked changes in the profile of phosphopolypeptides were observed primarily during the late exponential phase of growth. Several phosphopolypeptides co-purified with the endotoxin crystal of this subspecies and the phosphoamino acid residue of the most abundant (Mr 25,000) phosphopolypeptide was identified as phosphothreonine. Comparison of the phosphopolypeptides in endotoxin crystals from several subspecies suggested that Mr 25,000 species might be a common component.
Authors:
G M Watson; N H Mann
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of general microbiology     Volume:  134     ISSN:  0022-1287     ISO Abbreviation:  J. Gen. Microbiol.     Publication Date:  1988 Sep 
Date Detail:
Created Date:  1989-09-13     Completed Date:  1989-09-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0375371     Medline TA:  J Gen Microbiol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  2559-65     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, University of Warwick, Coventry, UK.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Autoradiography
Bacillus thuringiensis / growth & development,  metabolism*
Bacterial Proteins / metabolism*
Bacterial Toxins*
Chromatography, Thin Layer
Electrophoresis, Polyacrylamide Gel
Endotoxins / biosynthesis*
Hemolysin Proteins
Phosphopeptides / metabolism*
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Bacterial Proteins; 0/Bacterial Toxins; 0/Endotoxins; 0/Hemolysin Proteins; 0/Phosphopeptides; 0/insecticidal crystal protein, Bacillus Thuringiensis

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