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Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases
Author(s) -
Potempa Jan,
Golonka Ewa,
Filipek Renata,
Shaw Lindsey N.
Publication year - 2005
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2005.04714.x
Subject(s) - proteases , biology , gene , lipocalin , streptococcus pyogenes , genome , cysteine protease , bacteria , cytoplasm , cysteine , biochemistry , enzyme , microbiology and biotechnology , genetics , staphylococcus aureus
Summary 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.