Imperial College London
Alternate

Professor Martin Buck FRS

Faculty of Natural Sciences, Department of Life Sciences

Senior Research Investigator
 
 
 
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Contact

 

+44 (0)20 7594 5442m.buck

 
 
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Location

 

448Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Buck:2016:10.1016/j.bbamem.2016.10.018,
author = {Buck, M and Mcdonald, C and Jovanovic, G and Wallace, BA and Ces, O},
doi = {10.1016/j.bbamem.2016.10.018},
journal = {BBA Biomembranes},
pages = {28--39},
title = {Structure and function of PspA and Vipp1 N-terminal peptides:Insights into the membrane stress sensing and mitigation},
url = {http://dx.doi.org/10.1016/j.bbamem.2016.10.018},
volume = {1859},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The  phage  shock  protein  (Psp) response  maintains  integrity  ofthe innermembrane (IM) in responsetoextracytoplasmic stress conditionsand   is   widely   distributed amongstenterobacteria.  Its  central  componentPspA, a  member  of  the  IM30 peripheral  membrane protein family, acts asa major effector of the systemthrough its direct association with the IM. Under non-stress conditions PspA also negatively regulates its own expression via direct interaction  with  the  AAA+  ATPase  PspF.  PspA hasa  counterpart  in  cyanobacteria  calledVipp1, which  is implicated  in protection  of  the thylakoid  membranes. PspA’s  and  Vipp1’s conservedN-terminal regions  contain  a  putative amphipathic helix  a  (AHa)  required  for membranebinding.Anadjacent amphipathic helix b (AHb) in PspAis required for imposing negative control uponPspF.Here, purified peptides derived from the putative AH regions of PspA  and  Vipp1were  used  to  directly  probe their  effectorand  regulatory  functions.We observed  direct  membrane-binding  of AHaderived  peptides  and  an  accompanying  change in  secondary  structure  from unstructuredto alpha-helical establishing  them  as bonafidemembrane-sensing AH’s. The peptide-binding  specificitiesand  theireffects  on  membrane stability depend  onmembrane  anionic  lipid  content  and stored  curvature  elastic stress,in agreement withfull length PspA and Vipp1 proteinfunctionalities. AHbof PspA inhibited the ATPase activity of PspF demonstratingits direct regulatory role. These findings provide new insight  into  the  membrane  binding  and  function  of PspA  and  Vipp1and establish that synthetic peptides can be used to probe the structure-function of the IM30 protein family.
AU  - Buck,M
AU  - Mcdonald,C
AU  - Jovanovic,G
AU  - Wallace,BA
AU  - Ces,O
DO  - 10.1016/j.bbamem.2016.10.018
EP  - 39
PY  - 2016///
SN  - 0005-2736
SP  - 28
TI  - Structure and function of PspA and Vipp1 N-terminal peptides:Insights into the membrane stress sensing and mitigation
T2  - BBA Biomembranes
UR  - http://dx.doi.org/10.1016/j.bbamem.2016.10.018
UR  - http://hdl.handle.net/10044/1/42244
VL  - 1859
ER  -
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