Open AccessThe N 5 -Glutamine S -Adenosyl- l -Methionine-Dependent Methyltransferase PrmC/HemK in Chlamydia trachomatis Methylates Class 1 Release Factors
Author(s) -
Yvonne Pannekoek,
Valérie HeurguéHamard,
Ankie A. J. Langerak,
Dave Speijer,
Richard H. Buckingham,
Arie van der Ende
Publication year - 2005
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.187.2.507-511.2005
Subject(s) - biology , methylation , chlamydia trachomatis , methyltransferase , escherichia coli , glutamine , microbiology and biotechnology , glutamine synthetase , methionine , recombinant dna , in vivo , biochemistry , gene , amino acid , genetics , virology
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.