Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts

Szeto, T. H., Rowland, S. L., Rothfield, L. I. and King, G. F. (2002) Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts. Proceedings of The National Academy of Sciences of The United States of America, 99 24: 15693-15698. doi:10.1073/pnas.232590599


Author Szeto, T. H.
Rowland, S. L.
Rothfield, L. I.
King, G. F.
Title Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts
Journal name Proceedings of The National Academy of Sciences of The United States of America   Check publisher's open access policy
ISSN 0027-8424
Publication date 2002
Sub-type Article (original research)
DOI 10.1073/pnas.232590599
Open Access Status Not Open Access
Volume 99
Issue 24
Start page 15693
End page 15698
Total pages 6
Place of publication Washington
Publisher Natl Acad Sciences
Language eng
Abstract MinD is a widely conserved ATPase that has been demonstrated to play a pivotal role in selection of the division site in eubacteria and chloroplasts. It is a member of the large ParA superfamily of ATPases that are characterized by a deviant Walker-type ATP-binding motif. MinD localizes to the cytoplasmic face of the inner membrane in Escherichia coli, and its association with the inner membrane is a prerequisite for membrane recruitment of the septation inhibitor MinC. However, the mechanism by which MinD associates with the membrane has proved enigmatic; it seems to lack a transmembrane domain and the amino acid sequence is devoid of hydrophobic tracts that might predispose the protein to interaction with lipids. In this study, we show that the extreme C-terminal region of MinD contains a highly conserved 8- to 12-residue sequence motif that is essential for membrane localization of the protein. We provide evidence that this motif forms an amphipathic helix that most likely mediates a direct interaction between MinD and membrane phospholipids. A model is proposed whereby the membrane-targeting motif mediates the rapid cycles of membrane attachment-release-reattachment that are presumed to occur during pole-to-pole oscillation of MinD in E coli.
Keyword Multidisciplinary Sciences
Bacterial-cell Division
To-pole Oscillation
Escherichia-coli
Bacillus-subtilis
Topological Regulation
Inhibitor Minc
Rapid Pole
Protein
Atpase
Septum
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Wed, 19 Sep 2007, 15:05:50 EST