Sporulation protein SpoIVFB from Bacillus subtilis enhances processing of the sigma factor precursor Pro-sigma K in the absence of other sporulation gene products.
Processing of inactive pro-sigma K to active sigma K in the mother cell compartment of sporulating Bacillus subtilis is governed by a signal transduction pathway emanating from the forespore and involving SpoIVFB in the mother cell. Coexpression of spoIVFB and sigK (encoding pro-sigma K) genes in growing B. subtilis or Escherichia coli enhanced pro-sigma K processing in the absence of other sporulation-specific gene products. The simplest explanation of these results is that SpoIVFB is a protease that processes pro-sigma K.
Department of Biochemistry, Michigan State University, East Lansing 48824.
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D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D010450:Endopeptidases; D004926:Escherichia coli / Q000235:genetics; D008565:Membrane Proteins; D009024:Morphogenesis; D010957:Plasmids / Q000235:genetics; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000378:metabolism; D012808:Sigma Factor / Q000378:metabolism / Q000633:toxicity; D015398:Signal Transduction; D013171:Spores, Bacterial / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D008565:Membrane Proteins; D011994:Recombinant Proteins; D012808:Sigma Factor; D010450:Endopeptidases; C071442:spoIVFB protein, Bacillus subtilis