Phosphorylation of proteins in Xanthomonas campestris pv. oryzae

Bei chang Yang, Yi fang Ho, Jun shang Liu, Tsong teh Kuo

研究成果: Article同行評審

3 引文 斯高帕斯(Scopus)

摘要

Protein phosphorylation was studied in Xanthomonas campestris pv. oryzae in vivo and in vitro. In vitro labelling showed that the protein kinases in this bacterium used both ATP and GTP as nucleotide substrates at nearly the same efficiency. At least 6 proteins were phosphorylated in vitro, including abundant species of p81, p44, and p32 with Mr of 81000, 44000, and 32000, respectively. Three types of phosphate-protein linkage were found in this bacterium: O-phosphate, N-phosphate and probably acyl phosphate. The p81 and p32 were phosphorylated at histidine. The p44 had mainly phosphoserine and a small part of phosphohistidine. The phosphorylation profile was variable depending on the growth conditions. Furthermore, by a virulent phage Xp10 infection the quantity of phosphorylation increased: for phosphohistinine more than 10-fold, and for phosphoserine about 3-fold. Thus, in this bacterium phosphorylation may be linked with a physiological regulation system and with Xp10 phage development.

原文English
頁(從 - 到)262-266
頁數5
期刊Archives of Microbiology
158
發行號4
DOIs
出版狀態Published - 1992 九月 1

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Biochemistry
  • Molecular Biology
  • Genetics

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