http://purl.uniprot.org/citations/10409639 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10409639 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10409639 | http://www.w3.org/2000/01/rdf-schema#comment | "We have identified a novel mitochondrial targeting signal in the precursor of the DNA helicase Hmi1p of Saccharomyces cerevisiae that is located at the C terminus of the protein. Similar to classical N-terminal presequences, this C-terminal targeting signal consists of a stretch of positively charged amino acids that has the potential to form an amphipathic alpha-helix. Deletion of the C-terminal 36 amino acids of helicase resulted in loss of import into mitochondria, while deletion of the N-terminal 40 amino acids had no effect. When C-terminal regions of the helicase were placed at the C terminus of a passenger protein, dihydrofolate reductase, the resulting fusion proteins were directed into the mitochondrial matrix, and the C-terminal region of helicase became proteolytically processed. Import of helicase occurs in a C-to N-terminal direction; it requires a membrane potential and the TIM17-23 translocase together with mitochondrial Hsp70. Helicase is the only mitochondrial matrix protein identified thus far with a cleavable targeting signal at its C terminus."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.30.20937"xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.30.20937"xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/author | "Lee C.M."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/author | "Lee C.M."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/author | "Neupert W."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/author | "Neupert W."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/author | "Stuart R.A."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/author | "Stuart R.A."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/author | "Sedman J."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/author | "Sedman J."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/pages | "20937-20942"xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/pages | "20937-20942"xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/title | "The DNA helicase, Hmi1p, is transported into mitochondria by a C-terminal cleavable targeting signal."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/title | "The DNA helicase, Hmi1p, is transported into mitochondria by a C-terminal cleavable targeting signal."xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/volume | "274"xsd:string |
http://purl.uniprot.org/citations/10409639 | http://purl.uniprot.org/core/volume | "274"xsd:string |
http://purl.uniprot.org/citations/10409639 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10409639 |
http://purl.uniprot.org/citations/10409639 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10409639 |