Format

Send to

Choose Destination
Biochim Biophys Acta. 2000 Jul 26;1475(3):353-9.

Structural and functional studies on an FtsH inhibitor from Bacillus subtilis.

Author information

1
School of Biological Sciences, Royal Holloway University of London, Engham, Surrey TW20 0EX, UK.

Abstract

The small 3 kDa SpoVM protein is essential for development of the spore in Bacillus subtilis. Genetic and biochemical experiments have shown that the function of SpoVM is to inhibit the proteolytic activity of FtsH during sporulation. We have used a combination of genetic and biophysical techniques to characterise the role of this small polypeptide. SpoVM was found to be widespread in Bacillus as well as in two Clostridia species, suggesting that SpoVM provides a common mechanism for inactivating the FtsH protease during spore differentiation. Using site-specific mutagenesis, we have identified C-terminal residues of SpoVM essential for biological activity. Analysis of SpoVM's structure showed that it is able to assume an alpha-helical conformation in the presence of a lipid interface which may be important in interacting with FtsH.

PMID:
10913836
DOI:
10.1016/s0304-4165(00)00089-1
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center