Molecular and Structural Basis of ESCRT-III Recruitment to Membranes during Archaeal Cell Division

Rachel Y. Samson; Takayuki Obita; Ben Hodgson; Michael K. Shaw; Parkson Lee Gau Chong; Roger L. Williams; Stephen D. Bell

doi:10.1016/j.molcel.2010.12.018

Molecular and Structural Basis of ESCRT-III Recruitment to Membranes during Archaeal Cell Division

Rachel Y. Samson, Takayuki Obita, Ben Hodgson, Michael K. Shaw, Parkson Lee Gau Chong, Roger L. Williams, Stephen D. Bell^*

^*Corresponding author for this work

Structural Biology

Research output: Contribution to journal › Article › peer-review

85 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	186-196
Number of pages	11
Journal	Molecular Cell
Volume	41
Issue number	2
DOIs	https://doi.org/10.1016/j.molcel.2010.12.018
State	Published - 2011/01/21

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2010.12.018

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title = "Molecular and Structural Basis of ESCRT-III Recruitment to Membranes during Archaeal Cell Division",

abstract = "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.",

author = "Samson, {Rachel Y.} and Takayuki Obita and Ben Hodgson and Shaw, {Michael K.} and Chong, {Parkson Lee Gau} and Williams, {Roger L.} and Bell, {Stephen D.}",

note = "Funding Information: The work was supported by Wellcome Trust Programme Grants (086045/Z/08/Z) to S.D.B. and (083639/Z/07/Z) to R.L.W. P.L.G.C. acknowledges the support from National Science Foundation (DMR-0706410). We thank the staff of Diamond beamline I02 for help with data collection, Olga Perisic for discussions and critical reading of the manuscript and Stefan Freund for assistance with NMR data collection. ",

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doi = "10.1016/j.molcel.2010.12.018",

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AU - Samson, Rachel Y.

AU - Obita, Takayuki

AU - Hodgson, Ben

AU - Shaw, Michael K.

AU - Chong, Parkson Lee Gau

AU - Williams, Roger L.

AU - Bell, Stephen D.

N1 - Funding Information: The work was supported by Wellcome Trust Programme Grants (086045/Z/08/Z) to S.D.B. and (083639/Z/07/Z) to R.L.W. P.L.G.C. acknowledges the support from National Science Foundation (DMR-0706410). We thank the staff of Diamond beamline I02 for help with data collection, Olga Perisic for discussions and critical reading of the manuscript and Stefan Freund for assistance with NMR data collection.

PY - 2011/1/21

Y1 - 2011/1/21

N2 - 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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Molecular and Structural Basis of ESCRT-III Recruitment to Membranes during Archaeal Cell Division

Abstract

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