| Literature DB >> 7751305 |
S M Najafi1, A C Willis, M D Yudkin.
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.Entities:
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Year: 1995 PMID: 7751305 PMCID: PMC176967 DOI: 10.1128/jb.177.10.2912-2913.1995
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490