Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity

Sonja-Verena Albers, Zalán Szabó, Arnold J.M. Driessen

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Abstract

A large number of secretory proteins in the thermoacidophile Sulfolobus solfataricus are synthesized as a precursor with an unusual leader peptide that resembles bacterial type IV prepilin signal sequences. This set of proteins includes the flagellin subunit but also various solute binding proteins. Here we describe the identification of the S. solfataricus homolog of bacterial type IV prepilin peptidases, termed MD. PibD is an integral membrane protein that is phylogenetically related to the bacterial enzymes. When heterologously expressed in Escherichia coli, PibD is capable of processing both the flagellin and glucose-binding protein (GlcS) precursors. Site-directed mutagenesis of the GlcS signal peptide shows that the substrate specificity of PibD is consistent with the variations found in proteins with type IV prepilin-like signal sequences of S. solfataricus. We conclude that PibD is responsible for the processing of these secretory proteins in S. solfataricus.

Original languageEnglish
Pages (from-to)3918 - 3925
Number of pages8
JournalJournal of Bacteriology
Volume185
Issue number13
DOIs
Publication statusPublished - Jul-2003

Keywords

  • METHANOCOCCUS-VOLTAE PREFLAGELLIN
  • AMINO-ACID SUBSTITUTIONS
  • COMPLETE GENOME SEQUENCE
  • PILIN LEADER PEPTIDASE
  • PSEUDOMONAS-AERUGINOSA
  • SULFOLOBUS-SOLFATARICUS
  • BIFUNCTIONAL ENZYME
  • N-METHYLTRANSFERASE
  • ESCHERICHIA-COLI
  • BINDING-PROTEIN

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