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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
1994-11-4
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pubmed:abstractText |
Previously we have shown that the first hydrophobic domain of leader peptidase (lep) can function to translocate a short N-terminal 18 residue antigenic peptide from the phage Pf3 coat protein across the plasma membrane of Escherichia coli. We have now examined the mechanism of insertion of N-terminal periplasmic tails and have defined the features needed to translocate these regions. We find that short tails of up to 38 residues are efficiently translocated in a SecA- and SecY-independent manner while longer tails are very poorly inserted. Efficient translocation of a 138 residue tail is restored and is Sec-dependent by the addition of a leader sequence to the N-terminus of the protein. We also find that while there is no amphiphilic helix requirement for N-terminal translocation, there is a charge requirement that is needed within the tail; an arginine and lysine residue can inhibit or completely block translocation when introduced into the tail region. Intriguingly, the membrane potential is required for insertion of a 38 residue tail but not for a 23 residue tail.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-104291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-1530939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-1885584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-1915262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2119256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2146683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2162353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2196172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2200169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2205394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2594779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2663841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2676512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2677637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2677744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2762295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-2847924,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-3024162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-3036831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-3308874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-3317413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-3544218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-3881443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-4007491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-4208134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-4594039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-6225933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-6282859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-6368003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-6756294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-6986388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-7039847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-812694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-8357800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-8405397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-8440259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7925307-8459445
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Capsid Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SecA protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/SecY protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/major coat protein, Pseudomonas...,
http://linkedlifedata.com/resource/pubmed/chemical/type I signal peptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4662-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7925307-Adenosine Triphosphatases,
pubmed-meshheading:7925307-Amino Acid Sequence,
pubmed-meshheading:7925307-Bacterial Proteins,
pubmed-meshheading:7925307-Biological Transport,
pubmed-meshheading:7925307-Capsid,
pubmed-meshheading:7925307-Capsid Proteins,
pubmed-meshheading:7925307-Electrophysiology,
pubmed-meshheading:7925307-Endopeptidases,
pubmed-meshheading:7925307-Escherichia coli,
pubmed-meshheading:7925307-Escherichia coli Proteins,
pubmed-meshheading:7925307-Membrane Proteins,
pubmed-meshheading:7925307-Membrane Transport Proteins,
pubmed-meshheading:7925307-Molecular Sequence Data,
pubmed-meshheading:7925307-Protein Conformation,
pubmed-meshheading:7925307-Protein Sorting Signals,
pubmed-meshheading:7925307-Recombinant Fusion Proteins,
pubmed-meshheading:7925307-Serine Endopeptidases,
pubmed-meshheading:7925307-Structure-Activity Relationship
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pubmed:year |
1994
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pubmed:articleTitle |
Translocation of N-terminal tails across the plasma membrane.
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pubmed:affiliation |
Department of Chemistry, Ohio State University, Columbus 43210.
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pubmed:publicationType |
Journal Article
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