PMID:12424340
| Citation |
Szeto, TH, Rowland, SL, Rothfield, LI and King, GF (2002) Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts. Proc. Natl. Acad. Sci. U.S.A. 99:15693-8 |
|---|---|
| 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. |
| Links |
PubMed PMC137778 Online version:10.1073/pnas.232590599 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Amino Acid Motifs; Amino Acid Sequence; Archaea/enzymology; Archaeal Proteins/chemistry; Bacteria/enzymology; Bacterial Proteins/chemistry; Cell Membrane/enzymology; Chloroplasts/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Evolution, Molecular; Membrane Proteins/chemistry; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Plant Proteins/chemistry; Protein Structure, Secondary; Protein Transport; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity |
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