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PMID: 7751305 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Site of phosphorylation of SpoIIAA, the anti-anti-sigma factor for sporulation-specific sigma F of Bacillus subtilis.

Journal of bacteriology ·Vol. 177 ·No. 10 ·1995-05-00 ·Pages 2912-3

Najafi SM, Willis AC, Yudkin MD

Abstract

Sigma F is regulated by an anti-sigma factor, SpoIIAB, and an anti-anti-sigma factor, SpoIIAA. SpoIIAB also functions as a phosphokinase which transfers phosphate from ATP to SpoIIAA; this phosphorylation is thought to be involved in the regulatory mechanism. By using [gamma-32P]ATP to phosphorylate SpoIIAA, cleaving the protein proteolytically, and analyzing the one resulting radiolabelled peptide by the Edman degradation procedure, we show that the site of phosphorylation in SpoIIAA is Ser-58.

MeSH Terms
Amino Acid Sequence Bacillus subtilis/metabolism Bacterial Proteins/antagonists & inhibitors,metabolism Molecular Sequence Data Phosphorylation Sequence Analysis Sigma Factor Spores, Bacterial/metabolism Transcription Factors
Chemicals
Bacterial Proteins FliA protein, Bacteria Sigma Factor Transcription Factors spoIIR protein, Bacillus subtilis spore-specific proteins, Bacillus
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Najafi S M
Department of Biochemistry, University of Oxford, United Kingdom.
Willis A C
Yudkin M D
References (10)
10 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1995-05-00
Pages
2912-3
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC176967
Subset
IM
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