Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-10-3
pubmed:databankReference
pubmed:abstractText
The Schizosaccharomyces pombe nuclear gene, atp2, encoding the beta subunit of the mitochondrial ATP synthase, was sequenced and found to contain a 1575-bp open reading frame. Two adjacent transcription-initiation sites were found at positions 34 and 44 nucleotides upstream of the translation-initiation codon. The deduced polypeptide sequence was composed of 525 amino acid residues (molecular mass = 56875 Da). The mature polypeptide starts at residue 45 (molecular mass = 51,685 Da), indicating the presence of a presequence of 44 residues, presumably involved in mitochondrial targeting. The atp2 mutant B59-1 [Boutry, M. & Goffeau, A. (1982) Eur. J. Biochem. 125, 471-477] and its related revertant allele R4-3 [Jault, J. M., Di Pietro, A., Falson, P., Gautheron, D. C., Boutry, M. & Goffeau, A. (1989) Biochem. Biophys. Res. Commun. 158, 392-399] were also cloned and sequenced. A single nonsense mutation, CAG (Gln170)----TAG (stop) in mutant B59-1, became a missense mutation, TAG (stop)----TAC (Tyr) in revertant R4-3. Gln170 is located between the first and second elements belonging to the nucleotide-binding site. Its substitution by a tyrosine residue increases the enzyme affinity towards ADP, the amount of endogenous nucleotides and the apparent negative cooperativity for ATPase activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
200
pubmed:geneSymbol
atp2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
61-7
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Beta subunit of mitochondrial F1-ATPase from the fission yeast. Deduced sequence of the wild type protein and identification of a mutation that increases nucleotide binding.
pubmed:affiliation
Unité de Biochimie Physiologique, Université Catholique de Louvain, Louvain-La-Neuve, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't