Publication Date:
2013-07-03
Description:
Porins are beta-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3856478/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3856478/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Housden, Nicholas G -- Hopper, Jonathan T S -- Lukoyanova, Natalya -- Rodriguez-Larrea, David -- Wojdyla, Justyna A -- Klein, Alexander -- Kaminska, Renata -- Bayley, Hagan -- Saibil, Helen R -- Robinson, Carol V -- Kleanthous, Colin -- 079605/Wellcome Trust/United Kingdom -- 079605/2/06/2/Wellcome Trust/United Kingdom -- 082045/Wellcome Trust/United Kingdom -- 294408/European Research Council/International -- BB/D008573/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/D00873/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/G020671/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G1000819/Medical Research Council/United Kingdom -- R0I HG003709/HG/NHGRI NIH HHS/ -- WT082045/Wellcome Trust/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2013 Jun 28;340(6140):1570-4. doi: 10.1126/science.1237864.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23812713" target="_blank"〉PubMed〈/a〉
Keywords:
Cell Membrane/metabolism
;
Colicins/chemistry/isolation & purification/*metabolism
;
Escherichia coli/chemistry/*metabolism
;
Escherichia coli Proteins/metabolism
;
Periplasmic Proteins/metabolism
;
Porins/*metabolism
;
Protein Multimerization
;
Protein Structure, Tertiary
;
Protein Transport
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
