Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
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.
Sir William Dunn School of Pathology, South Parks Road, Oxford OX1 3RE, UK.
Rachel Y
RY
Samson
Takayuki
T
Obita
Ben
B
Hodgson
Michael K
MK
Shaw
Parkson Lee-Gau
PL
Chong
Roger L
RL
Williams
Stephen D
SD
Bell
D019843:Archaeal Proteins / Q000032:analysis / Q000737:chemistry / Q000502:physiology*; D056827:Endosomal Sorting Complexes Required for Transport / Q000032:analysis / Q000737:chemistry / Q000502:physiology*; D019848:Gene Expression Regulation, Archaeal; D008081:Liposomes / Q000378:metabolism; D016366:Open Reading Frames; D017434:Protein Structure, Tertiary; D016944:Sulfolobus / Q000166:cytology*; D014158:Transcription, Genetic
D019843:Archaeal Proteins; D056827:Endosomal Sorting Complexes Required for Transport; D008081:Liposomes
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