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Specific protein phosphorylation induced in Xanthomonas campestris pv. oryzae by bacteriophage Xp12

Cheng, C.M.; Tu, J.; Yang, C.C.; Kuo, T.T.

Archives of Microbiology 161(4): 281-285

1994


ISSN/ISBN: 0302-8933
PMID: 8002710
DOI: 10.1007/bf00303581
Accession: 009442979

We have investigated the endogenous phosphorylation patterns of phosphorylated proteins of Xanthomonas campestris pv. oryzae induced by its bacteriophages. For bacteriophage Xp12-infected cells, at least three phosphoproteins with apparent molecular weights of 28, 28.5 and 45 kDa were detected by in vitro labeling with [gamma-32P]-ATP. These Xp12-specific phosphoproteins only occurred with Xp12 infection, and were not shown in uninfected or Xp10-infected cells. The protein kinase(s) responsible could use either ATP or GTP as the nucleotide substrate with nearly the same efficiency. Magnesium was proved to be an essential factor for the phosphorylation. EGTA treatment excluding the possibility that the presumed protein kinase was calcium-dependent. Under our reaction conditions, the optimal phosphorylation occurred at pH 7 to 8, for 30 to 40 min at 25 to 37 degrees C. The Xp12-specific protein phosphorylation hints at the existence of a physiological regulation mechanism involved in the life cycle of bacteriophage Xp12. Furthermore, the presumed protein kinase was shown to be encoded by the genome of Xp12 rather than indirectly induced by Xp12 infection.

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