title: Protein synthesis elongation factor Tu present in spores of Streptomyces coelicolor can be phosphorylated in vitro by the spore protein kinase.
abstract: In vitro phosphorylation of EF-Tu was shown in cell-free extract from dormant spores of Streptomyces coelicolor by a protein kinase present in spores. EF-Tu phosphorylation was observed on both intrinsic S. coelicolor factor and externally added purified EF-Tu from S. aureofaciens, on two isoforms. Putative serine and threonine residues as potential phosphorylation targets were determined in primary sequence and demonstrated on 3D structure model of EF-Tu.
authors.affiliation: Institute of Microbiology, Academy of Sciences of the Czech Republic, 142 20 Prague, Czechia.
authors.forename: M
authors.initials: M
authors.lastname: Holub
authors.forename: S
authors.initials: S
authors.lastname: Bezousková
authors.forename: L
authors.initials: L
authors.lastname: Kalachová
authors.forename: J
authors.initials: J
authors.lastname: Weiser
mesh_terms: D000595:Amino Acid Sequence; D015180:Electrophoresis, Gel, Two-Dimensional; D021621:Imaging, Three-Dimensional; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013171:Spores, Bacterial / Q000201:enzymology / Q000378:metabolism*; D013304:Streptomyces aureofaciens / Q000378:metabolism; D048372:Streptomyces coelicolor / Q000378:metabolism*
chemical_list: D011494:Protein Kinases; D010444:Peptide Elongation Factor Tu