Peptide Deformylase (def) is essential in Mycobacterium smegmatis, but the essentiality is compensated by inactivation of methionine formylation

Noga Naor, Omer Gadot, Michal Meir, Daniel Barkan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Background: Co-translational processes in bacteria are attractive drug targets, but while some processes are essential, others are not. The essentiality of Peptide Deformylase (PDF, def) for vitality of mycobacteria was speculated, but never unequivocally proven. Results: Here we show by targeted deletion experiments that def can only be deleted from M. smegmatis when an additional copy is present; that prior deletion of tRNAfMet-Formyl Transferase (FMT, encoded by fmt) renders def completely dispensable; and that re-introduction of fmt into a Δdef mutant is not possible-constituting a definitive proof for the essentiality of def in mycobacteria. Conclusions: Peptide deformylase is essential in M. smegmatis, but the fact that inactivation of fmt renders the gene completely dispensable, and thus any inhibitor of def useless, casts doubt on the usefulness of PDF as a drug-target in mycobacteria.

Original languageAmerican English
Article number232
JournalBMC Microbiology
Volume19
Issue number1
DOIs
StatePublished - 26 Oct 2019

Bibliographical note

Publisher Copyright:
© 2019 The Author(s).

Keywords

  • Co-translation
  • Formyl Transferase
  • Mycobacteria
  • Peptide Deformylase
  • Protein synthesis

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