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Subtilisin‐like autotransporter serves as maturation protease in a bacterial secretion pathway
Author(s) -
Coutte Loic,
Antoine Rudy,
Drobecq Hervé,
Locht Camille,
JacobDubuisson Françoise
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.18.5040
Subject(s) - biology , secretion , subtilisin , protease , chaperone (clinical) , serine protease , bordetella pertussis , biochemistry , bacterial outer membrane , extracellular , microbiology and biotechnology , bacteria , enzyme , escherichia coli , pathology , gene , medicine , genetics
Proteins of Gram‐negative bacteria destined to the extracellular milieu must cross the two cellular membranes and then fold at the appropriate time and place. The synthesis of a precursor may be a strategy to maintain secretion competence while preventing aggregation or premature folding (especially for large proteins). The secretion of 230 kDa filamentous haemagglutinin (FHA) of Bordetella pertussis requires the synthesis and the maturation of a 367 kDa precursor that undergoes the proteolytic removal of its ∼130 kDa C‐terminal intramolecular chaperone domain. We have identified a specific protease, SphB1, responsible for the timely maturation of the precursor FhaB, which allows for extracellular release of FHA. SphB1 is a large exported protein with a subtilisin‐like domain and a C‐terminal domain typical of bacterial autotransporters. SphB1 is the first described subtilisin‐like protein that serves as a specialized maturation protease in a secretion pathway of Gram‐negative bacteria. This is reminiscent of pro‐protein convertases of eukaryotic cells.