Structures of the DfsB protein family suggest a cationic, helical sibling lethal factor peptide

Taylor, Jonathan D, Taylor, Gabrielle, Hare, Stephen A and Matthews, Steve J (2016) Structures of the DfsB protein family suggest a cationic, helical sibling lethal factor peptide. Journal of Molecular Biology, 428 (3). pp. 554-560. ISSN 0022-2836

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Abstract

Bacteria have developed a variety of mechanisms for surviving harsh environmental conditions, nutrient stress and overpopulation. Paenibacillus dendritiformis produces a lethal protein (Slf) that is able to induce cell death in neighbouring colonies and a phenotypic switch in more distant ones. Slf is derived from the secreted precursor protein, DfsB, after proteolytic processing. Here, we present new crystal structures of DfsB homologues from a variety of bacterial species and a surprising version present in the yeast Saccharomyces cerevisiae. Adopting a four-helix bundle decorated with a further three short helices within intervening loops, DfsB belongs to a non-enzymatic class of the DinB fold. The structure suggests that the biologically active Slf fragment may possess a C-terminal helix rich in basic and aromatic residues that suggest a functional mechanism akin to that for cationic antimicrobial peptides.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Stephen Hare
Date Deposited: 21 Sep 2017 15:15
Last Modified: 21 Sep 2017 15:16
URI: http://sro.sussex.ac.uk/id/eprint/70275

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