We have cloned and sequenced the tuf1 gene from a kirromycin-producing strain of Streptomyces collinus. The gene encodes a polypeptide of 396 amino acid residues with a molecular weight of 43,849. The protein shows 97% identity with EF-Tu1 of S. coelicolor and is sensitive to kirromycin. EF-Tu-dependent translation of poly(U) was reduced to 50% in the presence of 0.25 microM kirromycin. Using high resolution two-dimensional electrophoresis and specific immunodetection with monoclonal antibodies we found that the EF-Tu1 is phosphorylated on threonine and that serine is the second phosphate-accepting amino acid. EF-Tu1 phosphorylated on threonine and serine residues was detected among the S150 supernatant proteins of vegetative cells, aerial mycelium and spores. The level of phosphorylated EF-Tu1 varied during the growth and differentiation.

Institute of Microbiology Academy of Sciences of the Czech Republic Prague

Citace poskytuje Crossref.org

General and molecular microbiology and microbial genetics in the IM CAS

Protein synthesis elongation factor Tu present in spores of Streptomyces coelicolor can be phosphorylated in vitro by the spore protein kinase

Post-translational modification(s) and cell distribution of Streptomyces aureofaciens translation elongation factor Tu overproduced in Escherichia coli

Protein kinase associated with ribosomes of streptomycetes

The role of GTP-binding proteins in mechanochemical movements of microorganisms and their potential to form filamentous structures