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Issue 6, 2012
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E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe–Phe bonds

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Abstract

YggG is a conserved lipoprotein localized to the outer membrane of Gram negative bacteria. Even though the expressed open reading frame has been identified previously, the Escherichia coli protein remained uncharacterized. We report that YggG of E. coli is a metalloprotease that cleaves its targets preferentially between Phe–Phe residues. Since the yggG promoter is upregulated when bacteria are subjected to media of low osmolarity, YggG was named LoiP (low osmolarity induced protease). LoiP has an intramolecular disulfide (S–S) bond that is formed even in the absence of the periplasmic oxido-reductase DsbA and proper membrane localization of LoiP can depend on another putative metalloprotease, YfgC.

Graphical abstract: E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe–Phe bonds

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Publication details

The article was received on 20 Dec 2011, accepted on 22 Mar 2012 and first published on 11 Apr 2012


Article type: Paper
DOI: 10.1039/C2MB05506F
Citation: Mol. BioSyst., 2012,8, 1775-1782
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    E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe–Phe bonds

    C. Lütticke, P. Hauske, U. Lewandrowski, A. Sickmann, M. Kaiser and M. Ehrmann, Mol. BioSyst., 2012, 8, 1775
    DOI: 10.1039/C2MB05506F

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