Open AccessProtein tyrosine phosphorylation in streptomycetes
Author(s) -
Waters Barbara,
Vujaklija Dusica,
Gold Michael R,
Davies Julian
Publication year - 1994
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.1574-6968.1994.tb07028.x
Subject(s) - tyrosine phosphorylation , protein tyrosine phosphatase , phosphorylation , tyrosine , biochemistry , protein phosphorylation , streptomyces hygroscopicus , biology , streptomyces , sh2 domain , receptor tyrosine kinase , streptomycetaceae , signal transduction , microbiology and biotechnology , bacteria , protein kinase a , actinomycetales , genetics
Using phosphotyrosine‐specific antibodies, we demonstrate that in several Streptomyces spp. a variety of proteins are phosphorylated on tyrosine residues. Tyrosine phosphorylation was found in a number of Streptomyces species including Streptomyces lividans, Streptomyces hygroscopicus and Streptomyces lavendulae . Each species exhibited a unique pattern of protein tyrosine phosphorylation. Moreover, the patterns of tyrosine phosphorylation varied during the growth phase and were also influenced by culture conditions. We suggest that metabolic shifts during the complex growth cycle of these filamentous bacteria, and possibly secondary metabolic pathways, may be controlled by the action of protein tyrosine kinases and phosphatases, as has been demonstrated in signal transduction pathways in eukaryotic organisms.