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Mol Cell. 2011 Jan 21;41(2):186-96. doi: 10.1016/j.molcel.2010.12.018.

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

Author information

1
Sir William Dunn School of Pathology, South Parks Road, Oxford OX1 3RE, UK.

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.

PMID:
21255729
PMCID:
PMC3763469
DOI:
10.1016/j.molcel.2010.12.018
[Indexed for MEDLINE]
Free PMC Article

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