TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway

JDH Jongbloed, U Martin, H Antelmann, M Hecker, H Tjalsma, G Venema, S Bron, JM van Dijl*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

133 Citations (Scopus)

Abstract

The recent discovery of a ubiquitous translocation pathway, specifically required for proteins with a twin-arginine motif in their signal peptide, has focused interest on its membrane-bound components, one of which is known as TatC. Unlike most organisms of which the genome has been sequenced completely, the Gram-positive eubacterium Bacillus subtilis contains two tatC-like genes denoted tatCd and tatCy. The corresponding TatCd and TatCy proteins have the potential to be involved in the translocation of 27 proteins with putative twin-arginine signal peptides of which similar to6-14 are likely to be secreted into the growth medium. Using a proteomic approach, we show that PhoD of B. subtilis, a phosphodiesterase belonging to a novel protein family of which all known members are synthesized with typical twin-arginine signal peptides, is secreted via the twin-arginine translocation pathway. Strikingly, TatCd is of major importance for the secretion of PhoD, whereas TatCy is not required for this process. Thus, TatC appears to be a specificity determinant for protein secretion via the Tat pathway, Based on our observations, we hypothesize that the TatC determined pathway specificity is based on specific interactions between TatC-like proteins and other pathway components, such as TatA, of which three paralogues are present in B. subtilis.

Original languageEnglish
Pages (from-to)41350-41357
Number of pages8
JournalThe Journal of Biological Chemistry
Volume275
Issue number52
Publication statusPublished - 29-Dec-2000

Keywords

  • SIGNAL PEPTIDASE-I
  • TEMPORALLY CONTROLLED EXPRESSION
  • COMPLETE GENOME SEQUENCE
  • BACILLUS-SUBTILIS
  • ESCHERICHIA-COLI
  • THYLAKOID MEMBRANE
  • ALKALINE-PHOSPHATASE
  • POLYACRYLAMIDE GELS
  • EXPORT PATHWAY
  • ALPHA-AMYLASE

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