In this section
@article{Taylor:2016:10.1016/j.jmb.2016.01.013,
author = {Taylor, J and Taylor, G and Hare, S and Matthews, SJ},
doi = {10.1016/j.jmb.2016.01.013},
journal = {Journal of Molecular Biology},
pages = {554--560},
title = {Structures of the DfsB protein family suggest a cationic, helical sibling-lethal factor peptide},
url = {http://dx.doi.org/10.1016/j.jmb.2016.01.013},
volume = {428},
year = {2016}
}
TY - JOUR
AB - Bacteria have developed a variety of mechanisms for survivingharsh environmental conditions, nutrient stress and overpopulation.Paenibacillus dendritiformis produces a lethal protein (Slf) that is ableto induce cell death in neighboring colonies and a phenotypic switch inmore distant ones. Slf is derived from the secreted precursor protein,DfsB, after proteolytic processing. Here, we present new crystalstructures of DfsB homologues from a variety of bacterial species and asurprising version present in the yeast Saccharomyces cerevisiae.Adopting a four-helix bundle decorated with a further three short heliceswithin intervening loops, DfsB belongs to a non-enzymatic class of theDinB fold. The structure suggests that the biologically-active Slffragment may possess a C-terminal helix rich in basic and aromaticresidues that suggest a functional mechanism akin to that for cationicantimicrobial peptides.
AU - Taylor,J
AU - Taylor,G
AU - Hare,S
AU - Matthews,SJ
DO - 10.1016/j.jmb.2016.01.013
EP - 560
PY - 2016///
SN - 1089-8638
SP - 554
TI - Structures of the DfsB protein family suggest a cationic, helical sibling-lethal factor peptide
T2 - Journal of Molecular Biology
UR - http://dx.doi.org/10.1016/j.jmb.2016.01.013
UR - http://hdl.handle.net/10044/1/28977
VL - 428
ER -
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