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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2005-8-31
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pubmed:abstractText |
Phage display was used to identify new components of the mammalian mitochondrial receptor complex using Tom20 as a binding partner. Two peptides were identified. One had partial identity (SMLTVMA) with a bacterial signal peptide from Toho-1, a periplasmic protein. The other had partial identity with a mitochondrial inner membrane glutamate carrier. The bacterial signal peptide could carry a protein into mitochondria both in vivo and in vitro. The first six residues of the sequence, SMLTVM, were necessary for import but the two adjacent arginine residues in the 30-amino-acid leader were not critical for import. The signal peptides of Escherichia coli beta-lactamase and Bacillsus subtilis lipase could not carry proteins into mitochondria. Presumably, the Toho-1 leader can adopt a structure compatible for recognition by the import apparatus.
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pubmed:grant |
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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/Amino Acid Transport System X-AG,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Lactamases,
http://linkedlifedata.com/resource/pubmed/chemical/beta-lactamase Toho-1, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/enhanced green fluorescent protein
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1420-682X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
62
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1890-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16041565-Amino Acid Sequence,
pubmed-meshheading:16041565-Amino Acid Transport System X-AG,
pubmed-meshheading:16041565-Bacillus subtilis,
pubmed-meshheading:16041565-Escherichia coli,
pubmed-meshheading:16041565-Escherichia coli Proteins,
pubmed-meshheading:16041565-Green Fluorescent Proteins,
pubmed-meshheading:16041565-HeLa Cells,
pubmed-meshheading:16041565-Humans,
pubmed-meshheading:16041565-Intracellular Membranes,
pubmed-meshheading:16041565-Lipase,
pubmed-meshheading:16041565-Membrane Potentials,
pubmed-meshheading:16041565-Mitochondria,
pubmed-meshheading:16041565-Mitochondrial Proteins,
pubmed-meshheading:16041565-Molecular Sequence Data,
pubmed-meshheading:16041565-Oligopeptides,
pubmed-meshheading:16041565-Peptide Library,
pubmed-meshheading:16041565-Protein Binding,
pubmed-meshheading:16041565-Protein Sorting Signals,
pubmed-meshheading:16041565-Protein Transport,
pubmed-meshheading:16041565-Recombinant Fusion Proteins,
pubmed-meshheading:16041565-beta-Lactamases
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pubmed:year |
2005
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pubmed:articleTitle |
Bacterial signal peptide recognizes HeLa cell mitochondrial import receptors and functions as a mitochondrial leader sequence.
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pubmed:affiliation |
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-2063, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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