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The N⁵-Glutamine S-Adenosyl-L-Methionine-Dependent Methyltransferase PrmC/HemK in Chlamydia trachomatis Methylates Class 1 Release Factors

Academic Medical Center, Departments of Medical Microbiology,¹ Biochemistry, University of Amsterdam, Amsterdam, The Netherlands,³ Institut de Biologie Physico-Chimique, Service de Biochimie-UPR 9073 CNRS, Paris, France²

Received 18 May 2004/ Accepted 24 September 2004

The gene prmC, encoding the putative S-adenosyl-L-methionine (AdoMet)-dependent methyltransferase (MTase) of release factors (RFs) of the obligate intracellular pathogen Chlamydia trachomatis, was functionally analyzed. Chlamydial PrmC expression suppresses the growth defect of a prmC knockout strain of Escherichia coli K-12, suggesting an interaction of chlamydial PrmC with E. coli RFs in vivo. In vivo methylation assays carried out with recombinant PrmC and RFs of chlamydial origin demonstrated that PrmC methylates RFs within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln. This is consistent with the enzymatic properties of PrmC of E. coli origin. We conclude that C. trachomatis PrmC functions as an N⁵-glutamine AdoMet-dependent MTase, involved in methylation of RFs.