Identification of residues essential for the catalytic activity of Sec11b, one of the two type I signal peptidases of Haloferax volcanii

Eyal Fink-Lavi, Jerry Eichler

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Sec11b is one of two signal peptidases (SPases) in the haloarchaeon Haloferax volcanii. Site-directed mutagenesis revealed Ser-72, His-137 and Asp-187 as essential for signal peptide cleavage. Thus, like the SPase of the methanoarchaeon Methanococcus voltae, H. volcanii Sec11b uses a catalytic mechanism reminiscent of its eukaryal rather than its bacterial counterpart. The availability of an additional model system to study the archaeal SPase, now in the form of the purified protein, promises additional insight into the behavior of this enzyme.

Original languageEnglish
Pages (from-to)257-260
Number of pages4
JournalFEMS Microbiology Letters
Volume278
Issue number2
DOIs
StatePublished - 1 Jan 2008

Keywords

  • Archaea
  • Haloferax volcanii
  • Protein secretion
  • Signal peptidase
  • Signal peptides

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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