Open AccessProteins that interact with GTP in Streptomyces griseus and its possible implication in morphogenesis
Author(s) -
Itoh Masayoshi,
Penyige Andras,
Okamoto Susumu,
Ochi Kozo
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08006.x
Subject(s) - gtp' , streptomyces griseus , mutant , biochemistry , mycelium , biology , phosphorylation , gtp binding protein regulators , streptomycetaceae , strain (injury) , gel electrophoresis , streptomyces , actinomycetales , g protein , chemistry , microbiology and biotechnology , bacteria , genetics , signal transduction , botany , enzyme , anatomy , gene
By cross‐linking with [α‐ 32 P]GTP or [γ‐ 32 P]GTP with or without UV treatment, several proteins of Streptomyces griseus were shown to interact with GTP in specific ways. After gel electrophoresis, 19 bands of radioactivity were found; 12 bands were assigned as GTP‐binding proteins and 6 bands as phosphorylated proteins. One band was assumed to be a guanylylated protein. The profile of radioactive bands was similar between cells prepared from liquid or solid culture, but markedly different between growth phases. A mutant (strain M‐1) defective in aerial mycelium formation, which was originally found as a decoyinine‐resistant isolate, was found to have a different profile of phosphorylated proteins.