Linked Life Data

1993703

Source:http://linkedlifedata.com/resource/pubmed/id/1993703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1991-3-20
pubmed:databankReference
pubmed:abstractText
Several cDNAs encoding H-protein, a constituent of the glycine cleavage system, were cloned from chicken liver cDNA libraries with an antibody raised against rat H-protein or with a nick-translated cDNA of an immunoreactive clone. The structure of the H-protein cDNA consisting of 910 base pairs was determined using clones with an apparent overlap in the nucleotide sequence. The cDNA encodes the precursor form of H-protein that is comprised of 39 amino acid residues for a mitochondrial presequence and 125 amino acid residues for the mature protein, following a 5' untranslated region of 13 base pairs. There are two genuine consensus sequences for the cleavage/polyadenylation of the precursor H-protein mRNA in the 3' untranslated region of the cDNA sequence. We showed by comparison with the delta-aminolevulinate synthase gene that only one copy of the H-protein cDNA occurs in the haploid genome of the chicken. Nevertheless, two types of H-protein mRNAs, which differ by the length of their 3' untranslated region, are produced in liver. The chicken H-protein gene extends over 8 kilobase pairs on the genome and includes 5 exons that encode the entire cDNA sequence. Two AATAAA motifs are coded in the last exon of this gene, suggesting that the differently size H-protein mRNAs are produced by the alternative use of these motifs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3317-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1993703-Amino Acid Oxidoreductases, pubmed-meshheading:1993703-Amino Acid Sequence, pubmed-meshheading:1993703-Animals, pubmed-meshheading:1993703-Blotting, Northern, pubmed-meshheading:1993703-Carrier Proteins, pubmed-meshheading:1993703-Chickens, pubmed-meshheading:1993703-Cloning, Molecular, pubmed-meshheading:1993703-DNA, pubmed-meshheading:1993703-Exons, pubmed-meshheading:1993703-Glycine, pubmed-meshheading:1993703-Glycine Decarboxylase Complex H-Protein, pubmed-meshheading:1993703-Glycine Dehydrogenase (Decarboxylating), pubmed-meshheading:1993703-Introns, pubmed-meshheading:1993703-Molecular Sequence Data, pubmed-meshheading:1993703-Poly A, pubmed-meshheading:1993703-RNA, Messenger, pubmed-meshheading:1993703-Restriction Mapping, pubmed-meshheading:1993703-Sequence Homology, Nucleic Acid
pubmed:year
1991
pubmed:articleTitle
The glycine cleavage system. Occurrence of two types of chicken H-protein mRNAs presumably formed by the alternative use of the polyadenylation consensus sequences in a single exon.
pubmed:affiliation
Department of Biochemistry, Toyama Medical and Pharmaceutical University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't