Linked Life Data

8132489

Source:http://linkedlifedata.com/resource/pubmed/id/8132489

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-4-21
pubmed:abstractText
Phosphate and oxoglutarate carriers transport phosphate and oxoglutarate across the inner membranes of mitochondria in exchange for OH- and malate, respectively. Both carriers belong to the mitochondrial carrier protein family, characterized by a tripartite structure made up of related sequences about 100 amino acids in length. The results obtained on the topology of the phosphate and oxoglutarate carriers are consistent with the six alpha-helix model proposed by Saraste and Walker. In both carriers the N- and C-terminal regions are exposed toward the cytosol. In addition, the oxoglutarate carrier has been shown to be a dimer by means of crosslinking studies. The bovine and human genes coding for the oxoglutarate carrier are split into eight and six exons, respectively, and five introns are found to the same position in both genes. The bovine and human phosphate carrier genes have the same organization with nine exons separated by eight introns at exactly the same positions. The phosphate carrier of mammalian mitochondria is synthesized with a cleavable presequence, in contrast to the oxoglutarate carrier and the other members of the mitochondrial carrier family. The precursor of the phosphate carrier is efficiently imported, proteolytically processed, and correctly assembled in isolated mitochondria. The presequence-deficient phosphate carrier is imported with an efficiency of about 50% as compared with the precursor of the phosphate carrier and is correctly assembled, demonstrating that the mature portion of the phosphate carrier contains sufficient information for import and assembly into mitochondria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0145-479X
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
493-501
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8132489-Amino Acid Sequence, pubmed-meshheading:8132489-Animals, pubmed-meshheading:8132489-Carrier Proteins, pubmed-meshheading:8132489-Cattle, pubmed-meshheading:8132489-Genes, pubmed-meshheading:8132489-Humans, pubmed-meshheading:8132489-Intracellular Membranes, pubmed-meshheading:8132489-Ion Channels, pubmed-meshheading:8132489-Membrane Proteins, pubmed-meshheading:8132489-Membrane Transport Proteins, pubmed-meshheading:8132489-Mitochondria, pubmed-meshheading:8132489-Mitochondrial ADP, ATP Translocases, pubmed-meshheading:8132489-Mitochondrial Proteins, pubmed-meshheading:8132489-Molecular Sequence Data, pubmed-meshheading:8132489-Multigene Family, pubmed-meshheading:8132489-Phosphate-Binding Proteins, pubmed-meshheading:8132489-Protein Conformation, pubmed-meshheading:8132489-Rats, pubmed-meshheading:8132489-Sequence Alignment, pubmed-meshheading:8132489-Sequence Homology, Amino Acid
pubmed:year
1993
pubmed:articleTitle
Transmembrane topology, genes, and biogenesis of the mitochondrial phosphate and oxoglutarate carriers.
pubmed:affiliation
Department of Pharmaco-Biology, University of Bari, Italy.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't