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 language | English |
---|---|
Pages (from-to) | 257-260 |
Number of pages | 4 |
Journal | FEMS Microbiology Letters |
Volume | 278 |
Issue number | 2 |
DOIs | |
State | Published - 1 Jan 2008 |
Keywords
- Archaea
- Haloferax volcanii
- Protein secretion
- Signal peptidase
- Signal peptides
ASJC Scopus subject areas
- Microbiology
- Molecular Biology
- Genetics