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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.

SUBMITTER: Samson RY 

PROVIDER: S-EPMC3763469 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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

Samson Rachel Y RY   Obita Takayuki T   Hodgson Ben B   Shaw Michael K MK   Chong Parkson Lee-Gau PL   Williams Roger L RL   Bell Stephen D SD  

Molecular cell 20110101 2


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  ...[more]

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