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

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posted on 2023-06-09, 08:01 authored by Jonathan D Taylor, Gabrielle Taylor, Stephen Hare, Steve J Matthews
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.

History

Publication status

  • Published

File Version

  • Published version

Journal

Journal of Molecular Biology

ISSN

0022-2836

Publisher

Elsevier

Issue

3

Volume

428

Page range

554-560

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2017-09-21

First Open Access (FOA) Date

2017-09-21

First Compliant Deposit (FCD) Date

2017-09-21

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