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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-2-6
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pubmed:abstractText |
The voltage-dependent gating of the colicin channel involves a substantial structural rearrangement that results in the transfer of about 35% of the 200 residues in its pore-forming domain across the membrane. This transfer appears to represent an unusual type of protein translocation that does not depend on a large, multimeric, protein pore. To investigate the ability of this system to transport arbitrary proteins, we made use of a pair of strongly interacting proteins, either of which could serve as a translocated cargo or as a probe to detect the other. Here we show that both an 86-residue and a 134-residue hydrophilic protein inserted into the translocated segment of colicin A are themselves translocated and are functional on the trans side of the bilayer. The disparate features of these proteins suggest that the colicin channel has a general protein translocation mechanism.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-10074943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-10482528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-10611978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-10736310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-10966813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-11004207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-11111923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-11292342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-11331908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-1483475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-1691183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-1704440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-2467303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-2909895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-4444537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-7521016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-7577966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-7577967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-8090709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-8119982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-8125966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-8709151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-8868045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-9009197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-9169618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-9268373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-9425068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-9539735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-9687368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11830660-9718299
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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 |
Feb
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1286-91
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11830660-Amino Acid Sequence,
pubmed-meshheading:11830660-Binding Sites,
pubmed-meshheading:11830660-Codon,
pubmed-meshheading:11830660-Colicins,
pubmed-meshheading:11830660-Deoxyribonucleases,
pubmed-meshheading:11830660-Hydrogen-Ion Concentration,
pubmed-meshheading:11830660-Ion Channel Gating,
pubmed-meshheading:11830660-Lipid Bilayers,
pubmed-meshheading:11830660-Models, Biological,
pubmed-meshheading:11830660-Molecular Sequence Data,
pubmed-meshheading:11830660-Protein Conformation,
pubmed-meshheading:11830660-Protein Multimerization,
pubmed-meshheading:11830660-Protein Transport
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pubmed:year |
2002
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pubmed:articleTitle |
Translocation of a functional protein by a voltage-dependent ion channel.
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pubmed:affiliation |
Albert Einstein College of Medicine, Bronx, NY 10461, USA. slatin@aecom.yu.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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