Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-8-17
pubmed:abstractText
The intracellular sorting of newly synthesized precursor proteins (preproteins) to mitochondria depends on the "mitochondria-targeting sequence" (MTS), which is located at the amino termini of the preproteins. MTS is required, however, not only for targeting newly synthesized preproteins to mitochondria, but also for all the following steps along the mitochondrial protein import pathway. MTS of nascent preproteins is first recognized by a cytoplasmic molecular chaperone, MSF, and then by Tom70 and Tom20 of the mitochondrial outer membrane receptor complex, Tom5 and Tom40 of the outer membrane protein translocation machinery, Tim23 of the inner membrane protein translocation machinery, and finally the processing peptidase, MPP, in the matrix. MTS is a multi-role sorting sequence which specifically interacts with various components along the mitochondrial protein import pathway. Recognition of MTS at multiple steps during the import of preproteins may contribute to the strict sorting of proteins destined for mitochondria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Membrane Transport..., http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Prkcz protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TOM20 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/TOM5 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/TOM70 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/TOMM20 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Tom40 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Tomm20 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Ywhaz protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/mitochondrial import stimulation...
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
123
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1010-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9603986-14-3-3 Proteins, pubmed-meshheading:9603986-Amino Acid Sequence, pubmed-meshheading:9603986-Animals, pubmed-meshheading:9603986-Biological Transport, pubmed-meshheading:9603986-Carrier Proteins, pubmed-meshheading:9603986-Fungal Proteins, pubmed-meshheading:9603986-Humans, pubmed-meshheading:9603986-Membrane Proteins, pubmed-meshheading:9603986-Membrane Transport Proteins, pubmed-meshheading:9603986-Mitochondria, pubmed-meshheading:9603986-Mitochondrial Membrane Transport Proteins, pubmed-meshheading:9603986-Molecular Chaperones, pubmed-meshheading:9603986-Molecular Sequence Data, pubmed-meshheading:9603986-Proteins, pubmed-meshheading:9603986-Receptors, Cell Surface, pubmed-meshheading:9603986-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:9603986-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9603986-Sequence Analysis
pubmed:year
1998
pubmed:articleTitle
Mitochondria-targeting sequence, a multi-role sorting sequence recognized at all steps of protein import into mitochondria.
pubmed:affiliation
Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Fukuoka, 812-8582, Japan. omurat@mxs.meshnet.or.jp
pubmed:publicationType
Journal Article, Review