Structural highlights
Publication Abstract from PubMed
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.
Molecular and Structural Basis of ESCRT-III Recruitment to Membranes during Archaeal Cell Division.,Samson RY, Obita T, Hodgson B, Shaw MK, Chong PL, Williams RL, Bell SD Mol Cell. 2011 Jan 21;41(2):186-96. PMID:21255729[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Samson RY, Obita T, Hodgson B, Shaw MK, Chong PL, Williams RL, Bell SD. Molecular and Structural Basis of ESCRT-III Recruitment to Membranes during Archaeal Cell Division. Mol Cell. 2011 Jan 21;41(2):186-96. PMID:21255729 doi:10.1016/j.molcel.2010.12.018
