Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.

Members of the crenarchaeal kingdom, such as Sulfolobus, divide by binary fission yet lack genes for the otherwise near-ubiquitous tubulin and actin superfamilies of cytoskeletal proteins. Recent work has established that Sulfolobus homologs of the eukaryotic ESCRT-III and Vps4 components of the ESC...

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Main Authors: Samson, R, Obita, T, Hodgson, B, Shaw, M, Chong, P, Williams, R, Bell, S
Format: Journal article
Language:English
Published: 2011
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author Samson, R
Obita, T
Hodgson, B
Shaw, M
Chong, P
Williams, R
Bell, S
author_facet Samson, R
Obita, T
Hodgson, B
Shaw, M
Chong, P
Williams, R
Bell, S
author_sort Samson, R
collection OXFORD
description Members of the crenarchaeal kingdom, such as Sulfolobus, divide by binary fission yet lack genes for the otherwise near-ubiquitous tubulin and actin superfamilies of cytoskeletal proteins. Recent work has established that Sulfolobus homologs of the eukaryotic ESCRT-III and Vps4 components of the ESCRT machinery play an important role in Sulfolobus cell division. In eukaryotes, several pathways recruit ESCRT-III proteins to their sites of action. However, the positioning determinants for archaeal ESCRT-III are not known. Here, we identify a protein, CdvA, that is responsible for recruiting Sulfolobus ESCRT-III to membranes. Overexpression of the isolated ESCRT-III domain that interacts with CdvA results in the generation of nucleoid-free cells. Furthermore, CdvA and ESCRT-III synergize to deform archaeal membranes in vitro. The structure of the CdvA/ESCRT-III interface gives insight into the evolution of the more complex and modular eukaryotic ESCRT complex.
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spelling oxford-uuid:d6830a6d-b861-4d6c-b353-ac469a3e33fb2022-03-27T08:34:03ZMolecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d6830a6d-b861-4d6c-b353-ac469a3e33fbEnglishSymplectic Elements at Oxford2011Samson, RObita, THodgson, BShaw, MChong, PWilliams, RBell, SMembers of the crenarchaeal kingdom, such as Sulfolobus, divide by binary fission yet lack genes for the otherwise near-ubiquitous tubulin and actin superfamilies of cytoskeletal proteins. Recent work has established that Sulfolobus homologs of the eukaryotic ESCRT-III and Vps4 components of the ESCRT machinery play an important role in Sulfolobus cell division. In eukaryotes, several pathways recruit ESCRT-III proteins to their sites of action. However, the positioning determinants for archaeal ESCRT-III are not known. Here, we identify a protein, CdvA, that is responsible for recruiting Sulfolobus ESCRT-III to membranes. Overexpression of the isolated ESCRT-III domain that interacts with CdvA results in the generation of nucleoid-free cells. Furthermore, CdvA and ESCRT-III synergize to deform archaeal membranes in vitro. The structure of the CdvA/ESCRT-III interface gives insight into the evolution of the more complex and modular eukaryotic ESCRT complex.
spellingShingle Samson, R
Obita, T
Hodgson, B
Shaw, M
Chong, P
Williams, R
Bell, S
Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
title Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
title_full Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
title_fullStr Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
title_full_unstemmed Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
title_short Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
title_sort molecular and structural basis of escrt iii recruitment to membranes during archaeal cell division
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