The BON domain: A putative membrane-binding domain

The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, UK CB10 1SA.
Trends in Biochemical Sciences (Impact Factor: 11.23). 08/2003; 28(7):352-5. DOI: 10.1016/S0968-0004(03)00115-4
Source: PubMed


A novel conserved protein region – the BON (bacterial OsmY and nodulation) domain – is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. Functional annotation in the literature suggests that it interacts with phospholipid membranes. A lack of catalytic residues in the sequence alignment supports the hypothesis that it is a binding domain.

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    • "ygaU encodes an uncharacterized protein demonstrated to be induced by salt stress in E. coli[27] and to be a novel member of the RpoS regulon in S. Typhimurium [28]. It contains a BON domain, which is characteristic of osmotic shock protection proteins [29], and a LysM domain, which was first reported in bacterial cell wall degrading enzymes and recently in other proteins with a variety of functions [30]. In the current investigation, ygaU was found to be significantly regulated in eight tested conditions, but due to our difficulties with construction of a defined mutant we could not assess the importance for stress adaptation. "
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    • "PSI-BLAST searches confirm that EscD also contains a cytoplasmic FHA domain (Figure 2). In addition, these searches revealed the presence of at least one putative phospholipid-binding domain (also called a BON domain [53]) in the periplasmic portion of the protein (Figure 3). Two compelling hypotheses arise from these observations. "
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