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...
Main Authors: | , , , , , , |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2011
|
_version_ | 1797097446561546240 |
---|---|
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. |
first_indexed | 2024-03-07T04:55:37Z |
format | Journal article |
id | oxford-uuid:d6830a6d-b861-4d6c-b353-ac469a3e33fb |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T04:55:37Z |
publishDate | 2011 |
record_format | dspace |
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 |
work_keys_str_mv | AT samsonr molecularandstructuralbasisofescrtiiirecruitmenttomembranesduringarchaealcelldivision AT obitat molecularandstructuralbasisofescrtiiirecruitmenttomembranesduringarchaealcelldivision AT hodgsonb molecularandstructuralbasisofescrtiiirecruitmenttomembranesduringarchaealcelldivision AT shawm molecularandstructuralbasisofescrtiiirecruitmenttomembranesduringarchaealcelldivision AT chongp molecularandstructuralbasisofescrtiiirecruitmenttomembranesduringarchaealcelldivision AT williamsr molecularandstructuralbasisofescrtiiirecruitmenttomembranesduringarchaealcelldivision AT bells molecularandstructuralbasisofescrtiiirecruitmenttomembranesduringarchaealcelldivision |