Specific Targeting of the Metallophosphoesterase YkuE to the Bacillus Cell Wall Requires the Twin-arginine Translocation System

Carmine G. Monteferrante, Marcus Miethke, Rene van der Ploeg, Corinna Glasner, Jan Maarten van Dijl*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

20 Citations (Scopus)

Abstract

The twin-arginine translocation (Tat) pathway is dedicated to the transport of fully folded proteins across the cytoplasmic membranes of many bacteria and the chloroplast thylakoidal membrane. Accordingly, Tat-dependently translocated proteins are known to be delivered to the periplasm of Gram-negative bacteria, the growth medium of Gram-positive bacteria, and the thylakoid lumen. Here, we present the first example of a protein, YkuE of Bacillus subtilis, that is specifically targeted by the Tat pathway to the cell wall of a Gram-positive bacterium. The cell wall binding of YkuE is facilitated by electrostatic interactions. Interestingly, under particular conditions, YkuE can also be targeted to the cell wall in a Tat-independent manner. The biological function of YkuE was so far unknown. Our present studies show that YkuE is a metal-dependent phosphoesterase that preferentially binds manganese and zinc.

Original languageEnglish
Pages (from-to)29789-29800
Number of pages12
JournalThe Journal of Biological Chemistry
Volume287
Issue number35
DOIs
Publication statusPublished - 24-Aug-2012

Keywords

  • BACTERIAL CYTOPLASMIC MEMBRANE
  • SUBTILIS TAT PATHWAY
  • PROTEIN SECRETION
  • ESCHERICHIA-COLI
  • SIGNAL PEPTIDES
  • ALKALINE-PHOSPHATASE
  • STREPTOCOCCUS-PNEUMONIAE
  • STREPTOMYCES-COELICOLOR
  • FOLDED PROTEINS
  • EXPORT PATHWAY

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