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A conserved ClpP ‐like protease involved in spore outgrowth in B acillus subtilis
Author(s) -
Traag Bjorn A.,
Pugliese Antonia,
Setlow Barbara,
Setlow Peter,
Losick Richard
Publication year - 2013
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/mmi.12355
Subject(s) - bacillus subtilis , proteases , biology , protease , mutant , serine protease , spore , spore germination , endospore , biochemistry , microbiology and biotechnology , bacteria , gene , enzyme , genetics
Summary Germination and outgrowth of endospores of the G ram‐positive bacterium B acillus subtilis involves the degradation and conversion to free amino acids of abundant proteins located in the spore core known as small acid‐soluble proteins ( SASP ). This degradation is mediated primarily by the germination protease Gpr . Here we show that YmfB , a distant homologue of ClpP serine proteases that is highly conserved among endospore‐forming bacteria, contributes to SASP degradation but that its function is normally masked by Gpr . Spores from a ymfB gpr double mutant were more delayed in spore outgrowth and more impaired in SASP degradation than were spores from a gpr single mutant. The activity of YmfB relied on three putative active‐site residues as well as on the product of a small gene ylzJ located immediately downstream of, and overlapping with, ymfB . We propose that YmfB is an orphan ClpP protease that is dedicated to the degradation of a specialized family of small protein substrates.