Reference - Detail
|Author||Lütticke C, Hauske P, Lewandrowski U, Sickmann A, Kaiser M, Ehrmann M.|
|Title||E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.|
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.
|MeSH||Cell Membrane / chemistry Cell Membrane / metabolism Cytoskeletal Proteins / chemistry Cytoskeletal Proteins / metabolism Dipeptides / chemistry Dipeptides / metabolism* Escherichia coli Proteins / chemistry Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism* Hydrolysis Metalloproteases / chemistry Metalloproteases / genetics Metalloproteases / metabolism*|
|WOS Category||BIOCHEMISTRY & MOLECULAR BIOLOGY|
|Prokaryotes E. coli||NA|