|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:dateCreated |
2002-11-27
|
|
pubmed:abstractText |
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.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10220403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10503244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10515933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10529196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10540287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10619014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10619015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10633093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10690414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10764749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10801439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10931335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-10931339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11044440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11102868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11121066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11148270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11248256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11296216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11430835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11461697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11591668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11752455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11800381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-11983867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-1836760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-2211516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-2645057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-7990966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-8445645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-8810902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-9054497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-9109679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-9790530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12424340-9808628
|
|
pubmed:language |
eng
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:author |
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
15693-8
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:articleTitle |
Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts.
|
|
pubmed:affiliation |
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, 06032, USA.
|
