Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases.
The genes encoding secreted, broad-spectrum activity cysteine proteases of Staphylococcus spp. (staphopains) and Streptococcus pyogenes (streptopain, SpeB) are genetically linked to genes encoding cytoplasmic inhibitors. While staphopain inhibitors have lipocalin-like folds, streptopain is inhibited by a protein bearing the scaffold of the enzyme profragment. Bioinformatic analysis of other prokaryotic genomes has revealed that two more species may utilize this same genetic arrangement to control streptopain-like proteases with lipocalin-like inhibitors, while three other species may employ a C-terminally located domain that resembles the profragment. This apparently represents a novel system that bacteria use to control the intracellular activity of their proteases.
Potempa
Jan
J
Department of Microbiology, Faculty of Biotechnology, Jagiellonian University, ul. Gronostajowa 7, 30-387 Kraków, Poland. potempa@uga.edu
Golonka
Ewa
E
Filipek
Renata
R
Shaw
Lindsey N
LN
D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; D015853:Cysteine Proteinase Inhibitors; D003546:Cysteine Endopeptidases