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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 tRNA fMet -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.

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