[Identification of a sulfhydryl-reducing agent-inducible protein highly homologous to protein synthesis elongation factor Tu in Bacillus subtilis].
It was examined that the effect of beta-mercaptoethanol and dithiothreitol treatments, which should affect disulfide bond formation of proteins, on cellular protein components of Bacillus subtilis. In LB medium, the treatments induced the synthesis of a 50 kD protein (P50), which is synthesized constitutively under normal growth condition and is a major cytoplasmic protein. P50 was also induced by heat shock, but not by sporulation. In Schaeffer's sporulation medium, however, P50 was not induced by the sulfhydryl-reducing agents. This suggests that the sulfhydryl-reducing agent-inducibility of P50 might depent on specific physiological condition(s). The amino terminal sequences of two of the four main V8 protease fragments of P50 were determined. A search in databases revealed that P50 was highly homologous to protein synthesis elongation factor Tu of B. subtilis.
Wang
T
T
Institute of Botany, Chinese Academy of Sciences, Beijing 100093.
Kadokura
H
H
Yada
K
K
Yamasaki
M
M
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000187:drug effects / Q000502:physiology*; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000737:chemistry; D004229:Dithiothreitol / Q000494:pharmacology; D008623:Mercaptoethanol / Q000494:pharmacology; D010444:Peptide Elongation Factor Tu / Q000096:biosynthesis* / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013171:Spores, Bacterial / Q000502:physiology; D013439:Sulfhydryl Reagents / Q000494:pharmacology*
D001426:Bacterial Proteins; D013439:Sulfhydryl Reagents; D008623:Mercaptoethanol; D010444:Peptide Elongation Factor Tu; D004229:Dithiothreitol