Evidence that the Bacillus subtilis SpoIIGA protein is a novel type of signal-transducing aspartic protease.
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SpoIIR is a putative forespore-made signaling protein and SpoIIGA is a putative protease; together they are necessary and sufficient for accurate, rapid, and abundant processing of pro-sigma(E) to sigma(E), demonstrated by heterologous reconstitution in E. coli.
"expression of SpoIIR, a"
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SpoIIGA interacts with SpoIIR; the data support a model in which SpoIIR binding to the N-terminal (membrane) domain of SpoIIGA drives a conformational change that assembles an active aspartic-protease dimer in the C-terminal domain on the mother-cell side of the membrane, cleaving pro-sigma(E).
"SpoIIGA interacts with SpoIIR."