Linked Life Data

2894849

Source:http://linkedlifedata.com/resource/pubmed/id/2894849

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-5-5
pubmed:databankReference
pubmed:abstractText
The amino acid sequence of all but a few N-terminal residues of the beta subunit of rat liver ATP synthase has been determined from cDNA clones. Rat liver F1-beta is shown to contain 17 amino acid differences from that reported for F1-beta of bovine heart, 2 differences of which involve differences in charge. This may account in part for the observation that bovine heart F1 binds nucleotides with much greater affinity than the rat liver enzyme. Rat liver F1-beta also contains homologous regions with another nucleotide binding protein, adenylate kinase, for which high-resolution structural studies are available. Adjacent to one of these homologous regions is an eight amino acid stretch which bears striking homology to the phosphorylation region of the (Na+,K+)-ATPase. The combination of these two homology regions may constitute at least part of a nucleotide binding domain in F1-beta. Significantly, both rat liver and bovine heart beta contain these regions of homology, whereas the 17 amino acid differences between the two enzymes lie outside this region. The possibility of a second nucleotide binding domain which differs between the two enzymes is discussed. A cDNA clone containing all the regions of homology as well as 11 of the 17 amino acid differences between the bovine heart and rat liver beta subunits has been ligated into the bacterial expression vector pKK223-3. After transformation of a protease-deficient strain of Escherichia coli, this cDNA clone is expressed as a 36-kilodalton protein.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
553-60
pubmed:dateRevised
2008-4-21
pubmed:meshHeading
pubmed-meshheading:2894849-Adenylate Kinase, pubmed-meshheading:2894849-Amino Acid Sequence, pubmed-meshheading:2894849-Animals, pubmed-meshheading:2894849-Base Sequence, pubmed-meshheading:2894849-Cloning, Molecular, pubmed-meshheading:2894849-DNA, pubmed-meshheading:2894849-Escherichia coli, pubmed-meshheading:2894849-Genes, pubmed-meshheading:2894849-Macromolecular Substances, pubmed-meshheading:2894849-Mitochondria, Liver, pubmed-meshheading:2894849-Mitochondrial Proton-Translocating ATPases, pubmed-meshheading:2894849-Models, Molecular, pubmed-meshheading:2894849-Molecular Sequence Data, pubmed-meshheading:2894849-Phosphotransferases, pubmed-meshheading:2894849-Protein Conformation, pubmed-meshheading:2894849-Proton-Translocating ATPases, pubmed-meshheading:2894849-Rats, pubmed-meshheading:2894849-Receptors, Peptide, pubmed-meshheading:2894849-Sequence Homology, Nucleic Acid, pubmed-meshheading:2894849-Transcription, Genetic
pubmed:year
1988
pubmed:articleTitle
Beta subunit of rat liver mitochondrial ATP synthase: cDNA cloning, amino acid sequence, expression in Escherichia coli, and structural relationship to adenylate kinase.
pubmed:affiliation
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.