Specific in Vitro Guanylylation of a 43-kilodalton Membrane-associated Protein of Streptomyces Coelicolor

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1993 May 1

PMID 8491738

Citations 1

Authors

A J Obaya

J Guijarro

Affiliations

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Abstract

Incubation of [alpha-32P]GTP with cellular extracts or membranes of Streptomyces coelicolor labels a protein of 43 kDa, which was also labeled with [8,5'-3H]GTP but not with [alpha-32P]ATP or [gamma-32P]GTP. Radioactivity remained associated with this protein after boiling in 0.1 N NaOH, but it was dissociated after incubation in 0.1 N HCl or hydroxylamine. Chromatographic analysis of the HCl-dissociated compound showed that GMP was the covalently bound nucleotide. Furthermore, guanylylation appeared to be reversible and to take place by a pyrophosphorylytic mechanism. Guanylylation was more efficient at low temperatures. Several Streptomyces species showed a guanylylated protein with a similar molecular mass.

Citing Articles

Changes in patterns of ADP-ribosylated proteins during differentiation of Streptomyces coelicolor A3(2) and its development mutants.

Shima J, Penyige A, Ochi K J Bacteriol. 1996; 178(13):3785-90.

PMID: 8682781 PMC: 232637. DOI: 10.1128/jb.178.13.3785-3790.1996.

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