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REGULATION OF PROTEIN-PHOSPHORYLATION IN THE CYANOBACTERIUM ANABAENA STRAIN PCC-7120
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UNSPECIFIED. (1991) REGULATION OF PROTEIN-PHOSPHORYLATION IN THE CYANOBACTERIUM ANABAENA STRAIN PCC-7120. JOURNAL OF GENERAL MICROBIOLOGY, 137 (Part 2). pp. 331-339. ISSN 0022-1287
Full text not available from this repository.Abstract
Protein kinase activities have been detected in cell-free extracts of the cyanobacterium Anabaena PCC 7120. At least 12 polypeptides in the soluble fraction were phosphorylated in vitro at the expense of [gamma-32P]ATP and the pattern of phosphorylation was shown to be regulated by intermediary metabolites and other effectors, at physiological concentrations. Glucose 6-phosphate exerted a regulatory effect on a phosphopolypeptide of M(r) 56000 (p56) by stimulating a protein phosphatase, whereas ribulose 5-phosphate inhibited the corresponding protein kinase. In addition, DTT and the calmodulin antagonist trifluoperazine influenced the phosphorylation state of several different polypeptides, indicative of control by redox conditions and a calmodulin-like mediator, respectively. Furthermore, it was established that the phosphorylation of p56 required Mg2+ (> 100-mu-M) whereas that of a polypeptide of M(r) 16000 occurred in the absence of Mg2+ and was inhibited by high concentrations (> 1 mM) of this cation. Several of the phosphopolypeptides detected in vitro corresponded in mobility on SDS-PAGE to species phosphorylated in vivo.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QR Microbiology |
| Journal or Publication Title: | JOURNAL OF GENERAL MICROBIOLOGY |
| Publisher: | SOC GENERAL MICROBIOLOGY |
| ISSN: | 0022-1287 |
| Date: | February 1991 |
| Volume: | 137 |
| Number: | Part 2 |
| Number of Pages: | 9 |
| Page Range: | pp. 331-339 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/22865 |
Data sourced from Thomson Reuters' Web of Knowledge
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