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

• DOI: 10.1016/j.molcel.2010.12.018
• Publication Date: 2011-01-24T06:46:28Z
• Authors: Rachel Y. Samson; Takayuki Obita; Ben Hodgson; Michael K. Shaw; Parkson Lee-Gau C...; Roger L. Williams; Stephen D. Bell
• Keywords: 0303 health sciences; Endosomal Sorting Complexes Required for Transport; Transcription, Genetic; Archaeal Proteins; Cell Biology; Biochemistry; Protein Structure, Tertiary; Sulfolobus; Open Reading Frames; 03 medical and health sciences; Liposomes; Pathology; Gene Expression Regulation, Archaeal; Molecular Biology

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.