title: The N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase PrmC/HemK in Chlamydia trachomatis methylates class 1 release factors.
abstract: 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.
authors.affiliation: Academic Medical Center, Dept. of Medical Microbiology, Room L1-162, University of Amsterdam, PO Box 22660, 1100 DD Amsterdam, The Netherlands. y.pannekoek@amc.uva.nl
authors.forename: Yvonne
authors.initials: Y
authors.lastname: Pannekoek
authors.forename: Valérie
authors.initials: V
authors.lastname: Heurgué-Hamard
authors.forename: Ankie A J
authors.initials: AA
authors.lastname: Langerak
authors.forename: Dave
authors.initials: D
authors.lastname: Speijer
authors.forename: Richard H
authors.initials: RH
authors.lastname: Buckingham
authors.forename: Arie
authors.initials: A
authors.lastname: van der Ende
mesh_terms: D020816:Amino Acid Motifs; D001426:Bacterial Proteins / Q000378:metabolism*; D002692:Chlamydia trachomatis / Q000201:enzymology*; D017124:Conserved Sequence; D004269:DNA, Bacterial / Q000737:chemistry / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development; D017353:Gene Deletion; D005816:Genetic Complementation Test; D008745:Methylation; D008969:Molecular Sequence Data; D010454:Peptide Termination Factors / Q000378:metabolism*; D011496:Protein Methyltransferases / Q000378:metabolism*; D017422:Sequence Analysis, DNA
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D010454:Peptide Termination Factors; D011496:Protein Methyltransferases