Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.

The translocation of protein toxins into a cell relies on a myriad of protein-protein interactions. One such group of toxins are enzymatic E colicins, protein antibiotics produced by Escherichia coli in times of stress. These proteins subvert ordinary nutrient uptake mechanisms to enter the cell and...

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Main Authors: Bonsor, D, Meenan, N, Kleanthous, K
Format: Journal article
Language:English
Published: 2008
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author Bonsor, D
Meenan, N
Kleanthous, K
author_facet Bonsor, D
Meenan, N
Kleanthous, K
author_sort Bonsor, D
collection OXFORD
description The translocation of protein toxins into a cell relies on a myriad of protein-protein interactions. One such group of toxins are enzymatic E colicins, protein antibiotics produced by Escherichia coli in times of stress. These proteins subvert ordinary nutrient uptake mechanisms to enter the cell and unleash nuclease activity. We, and others, have previously shown that uptake of ColE9 (colicin E9) is dependent on engagement of the OM (outer membrane) receptors BtuB and OmpF as well as recruitment of the periplasmic protein TolB, forming a large supramolecular complex. Intriguingly, colicins bind TolB using a natively disordered region to mimic the interaction of TolB with Pal (peptidoglycan-associated lipoprotein). This is thought to trigger OM instability and prime the system for translocation. Here, we review key interactions in the assembly of this 'colicin translocon' and discuss the key role disorder plays in achieving uptake.
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spelling oxford-uuid:1c07dbbc-6874-48ee-8f1b-af83aabd65c52022-03-26T11:03:29ZColicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1c07dbbc-6874-48ee-8f1b-af83aabd65c5EnglishSymplectic Elements at Oxford2008Bonsor, DMeenan, NKleanthous, KThe translocation of protein toxins into a cell relies on a myriad of protein-protein interactions. One such group of toxins are enzymatic E colicins, protein antibiotics produced by Escherichia coli in times of stress. These proteins subvert ordinary nutrient uptake mechanisms to enter the cell and unleash nuclease activity. We, and others, have previously shown that uptake of ColE9 (colicin E9) is dependent on engagement of the OM (outer membrane) receptors BtuB and OmpF as well as recruitment of the periplasmic protein TolB, forming a large supramolecular complex. Intriguingly, colicins bind TolB using a natively disordered region to mimic the interaction of TolB with Pal (peptidoglycan-associated lipoprotein). This is thought to trigger OM instability and prime the system for translocation. Here, we review key interactions in the assembly of this 'colicin translocon' and discuss the key role disorder plays in achieving uptake.
spellingShingle Bonsor, D
Meenan, N
Kleanthous, K
Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.
title Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.
title_full Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.
title_fullStr Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.
title_full_unstemmed Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.
title_short Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.
title_sort colicins exploit native disorder to gain cell entry a hitchhiker s guide to translocation
work_keys_str_mv AT bonsord colicinsexploitnativedisordertogaincellentryahitchhikersguidetotranslocation
AT meenann colicinsexploitnativedisordertogaincellentryahitchhikersguidetotranslocation
AT kleanthousk colicinsexploitnativedisordertogaincellentryahitchhikersguidetotranslocation