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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1997-1-31
|
| pubmed:abstractText |
The gene encoding rat peptidylglycine alpha-amidating monooxygenase (PAM) contains 26 protein-coding exons. We identified two non-overlapping genomic clones encoding the 5' untranslated region (UTR) of the PAM gene. Exon 1 has 69 nucleotides flanked by perfect splice acceptor and donor sites, with a TATA motif 25 nucleotides upstream. Exon 0 lacks TATA or CAAT motifs and is embedded in a G + C-rich 800-nucleotide CpG island. The major products identified by RNase protection initiated in exon 0; only a minority of mRNAs initiated in exon 1. 5'-rapid amplification of cDNA ends (RACE) identified the same major transcriptional start sites in exon 0 in the atrium and neurointermediate pituitary. The 2.0-kb fragment upstream of exon 0 and the 1.3-kb fragment upstream of exon 1 were placed upstream of a luciferase-based reporter gene in both sense and antisense orientations. Expression of luciferase was observed in neuroendocrine and nonneuroendocrine cells with both sense constructs. A 0.2-kb fragment of the exon 0 PAM promoter containing multiple GC box elements supported expression of luciferase activity in all cell types. Expression of reporter genes in cells that do not normally express PAM suggests a need for more upstream or intronic information, a role for methylation, or a need for chromatin scaffolding for tissue-specific expression of the endogenous gene.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Recombinant,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/peptidylglycine monooxygenase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
1044-5498
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
15
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1093-104
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:8985123-Animals,
pubmed-meshheading:8985123-Base Sequence,
pubmed-meshheading:8985123-Cell Line,
pubmed-meshheading:8985123-Cloning, Molecular,
pubmed-meshheading:8985123-DNA, Complementary,
pubmed-meshheading:8985123-DNA, Recombinant,
pubmed-meshheading:8985123-Exons,
pubmed-meshheading:8985123-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:8985123-Genes,
pubmed-meshheading:8985123-Male,
pubmed-meshheading:8985123-Mixed Function Oxygenases,
pubmed-meshheading:8985123-Molecular Sequence Data,
pubmed-meshheading:8985123-Multienzyme Complexes,
pubmed-meshheading:8985123-Promoter Regions, Genetic,
pubmed-meshheading:8985123-RNA, Messenger,
pubmed-meshheading:8985123-Rats,
pubmed-meshheading:8985123-Rats, Sprague-Dawley,
pubmed-meshheading:8985123-Sequence Analysis, DNA,
pubmed-meshheading:8985123-Testis,
pubmed-meshheading:8985123-Transcription, Genetic
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Identification of the promoter for the gene encoding the bifunctional enzyme, peptidylglycine alpha-amidating monooxygenase.
|
| pubmed:affiliation |
Department of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|