Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-1-27
pubmed:databankReference
pubmed:abstractText
The sequences are presented of cDNAs encoding five related proteins from the nematode worm, Caenorhabditis elegans. Three of them can be recognised as the homologues of the ADP/ATP, phosphate and oxoglutarate/malate carrier proteins that have been found in the inner membranes of mitochondria in other species. These carrier proteins, and the uncoupling protein from the mitochondria in mammalian brown adipose tissue, have common features in their primary and secondary structures, and are members of the same protein super-family. Members of this super-family have polypeptide chains approximately 300 amino acid long that consist of three tandem related sequences of about 100 amino acids. The tandem repeats from the different proteins are inter-related, and each repeat is probably folded into a common secondary structural motif consisting of two hydrophobic stretches of amino acids with the potential to form membrane spanning alpha-helices, linked by an extensive hydrophilic region. The common characteristic features of this family of proteins are also present in sequences of two further proteins, named C1 and C2, encoded in nematode cDNAs, and in four published protein sequences from various sources. Neither the transport properties nor the subcellular locations of any of this latter group of six proteins are known. Therefore, currently the super-family of mitochondrial carrier proteins has at least ten different members.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1042-5179
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
281-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Extension of the mitochondrial transporter super-family: sequences of five members from the nematode worm, Caenorhabditis elegans.
pubmed:affiliation
M.R.C. Laboratory of Molecular Biology, Cambridge, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't