Abstract:
:The spoVM gene encodes a 26-amino-acid polypeptide that is essential for spore formation in Bacillus subtilis. A transposon insertion within the spoVM open reading frame has been shown to encode a chimeric protein which is biologically inactive and produces a phenotype identical to that of a deletion and insertion mutation. A genetic approach was used to identify possible interacting proteins, and the membrane-bound FtsH protease was identified. Mutations in ftsH suppressed the sporulation defect of certain spoVM mutants but not others. However, production of the mother cell sigma factors, sigmaE and sigmaK, was abnormal in the suppressed strains, and mutations in either spoVM or ftsH alone impaired sigma factor production and sporulation gene expression. Using FtsH purified from Escherichia coli, we demonstrated that in vitro (i) SpoVM inhibits FtsH protease activity and (ii) SpoVM is a substrate for the FtsH protease. We propose that during sporulation, SpoVM serves as a competitive inhibitor of FtsH activity. This interaction appears to be important for completion of the prespore engulfment step of sporulation, based on the phenotype of certain spoVM ftsH double mutants.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Cutting S,Anderson M,Lysenko E,Page A,Tomoyasu T,Tatematsu K,Tatsuta T,Kroos L,Ogura Tdoi
10.1128/jb.179.17.5534-5542.1997subject
Has Abstractpub_date
1997-09-01 00:00:00pages
5534-42issue
17eissn
0021-9193issn
1098-5530journal_volume
179pub_type
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