Specific in vitro guanylylation of a 43-kilodalton membrane-associated protein of Streptomyces coelicolor.
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.
Obaya
A J
AJ
Departamento de Biologia Funcional, Facultad de Medicina, Universidad de Oviedo, Spain.
Guijarro
J
J
D001426:Bacterial Proteins / Q000378:metabolism*; D001667:Binding, Competitive; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013045:Species Specificity; D013302:Streptomyces / Q000378:metabolism*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D008565:Membrane Proteins; D006160:Guanosine Triphosphate