The N 5 -Glutamine S -Adenosyl- l -Methionine-Dependent Methyltransferase PrmC/HemK in Chlamydia trachomatis Methylates Class 1 Release Factors-Reference-Cited by-同舟云学术

The N 5 -Glutamine S -Adenosyl- l -Methionine-Dependent Methyltransferase PrmC/HemK in Chlamydia trachomatis Methylates Class 1 Release Factors

Published:2005-01-15 Issue:2 Volume:187 Page:507-511
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Pannekoek Yvonne¹,Heurgué-Hamard Valérie²,Langerak Ankie A. J.¹,Speijer Dave³,Buckingham Richard H.²,van der Ende Arie¹

Affiliation:

1. Academic Medical Center, Departments of Medical Microbiology

2. Institut de Biologie Physico-Chimique, Service de Biochimie-UPR 9073 CNRS, Paris, France

3. Biochemistry, University of Amsterdam, Amsterdam, The Netherlands

Abstract

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 N 5 -glutamine AdoMet-dependent MTase, involved in methylation of RFs.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.187.2.507-511.2005

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