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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
1994-12-16
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pubmed:abstractText |
The Escherichia coli serine chemoreceptor takes on a simple membrane topology with two transmembrane segments separating cytoplasmically disposed N and C termini from a central periplasmic domain. We investigated the role of the small N-terminal cytoplasmic domain in membrane insertion using alkaline phosphatase gene fusions. Mutations eliminating the positive charge of the domain altered insertion dramatically, with reciprocal effects on hybrids with periplasmic and C-terminal cytoplasmic fusion junctions. Efficient export of the normally cytoplasmic C-terminal domain required that, in addition to the N-terminal changes, a short amphiphatic sequence at the beginning of the C-terminal domain be also absent. These findings document the importance of the positive character of the N-terminal domain in chemoreceptor membrane insertion and imply that partially redundant sequence information controls the orientation of the second transmembrane segment.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-1943817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-2153653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-2200169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-2205394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-2677744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-2820061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-2834370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-2846545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-3100913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-3323813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-3529391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961482-6402709
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
176
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7118-20
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7961482-Amino Acid Sequence,
pubmed-meshheading:7961482-Bacterial Proteins,
pubmed-meshheading:7961482-Escherichia coli,
pubmed-meshheading:7961482-Membrane Proteins,
pubmed-meshheading:7961482-Molecular Conformation,
pubmed-meshheading:7961482-Molecular Sequence Data,
pubmed-meshheading:7961482-Peptide Fragments,
pubmed-meshheading:7961482-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:7961482-Recombinant Fusion Proteins,
pubmed-meshheading:7961482-Serine
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pubmed:year |
1994
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pubmed:articleTitle |
Role of a small cytoplasmic domain in the establishment of serine chemoreceptor membrane topology.
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pubmed:affiliation |
Department of Genetics, University of Washington, Seattle 98195.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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