Source:http://linkedlifedata.com/resource/pubmed/id/10631802
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2000-2-16
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pubmed:databankReference | |
pubmed:abstractText |
The hepatic enzyme, glutamine synthetase (GSase) is a pivotal protein in the regulation of urea synthesis in fish. The sequence of the DNA encoding for GSase from liver of the ureotelic gulf toadfish (Opsanus beta) was analyzed through a suite of molecular techniques (including cDNA cloning, RACE PCR, and genomic PCR). An open reading frame (ORF) was identified in the cDNA sequence which codes for a protein of 394 amino acids with high identity (86%) to dogfish shark GSase. In the course of generating a suitable probe, a partial sequence was also obtained for horned shark GSase which also had high identity with the dogfish shark gene (93%). Like the dogfish shark GSase, the toadfish gene has two methionine translation initiation sites; the downstream site apparently codes for a cytoplasmic isozyme, while the upstream site adds an N-terminal peptide leader sequence of 23 amino acids to the 'cytoplasmic' protein. This leader sequence has characteristics consistent with a mitochondrial targeting peptide, including a cleavage recognition motif (Arg-X-Phe) and the apparent ability to form an amphiphathic helix. Northern analysis revealed that there is a single predominant transcript of approximately 2 kb in size. These results are consistent with the interpretation that in the gulf toadfish GSase cytoplasmic and mitochondrial isozymes are coded for by a single gene and mRNA transcript which is differentially translated at either initiation site. These results are discussed in the context of prior results for enzyme kinetic characteristics and urea synthesis/excretion physiology.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1096-4959
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
124
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
251-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10631802-Amino Acid Sequence,
pubmed-meshheading:10631802-Animals,
pubmed-meshheading:10631802-Base Sequence,
pubmed-meshheading:10631802-Blotting, Northern,
pubmed-meshheading:10631802-DNA, Complementary,
pubmed-meshheading:10631802-DNA Probes,
pubmed-meshheading:10631802-Evolution, Molecular,
pubmed-meshheading:10631802-Fishes,
pubmed-meshheading:10631802-Gene Library,
pubmed-meshheading:10631802-Glutamate-Ammonia Ligase,
pubmed-meshheading:10631802-Liver,
pubmed-meshheading:10631802-Molecular Sequence Data,
pubmed-meshheading:10631802-Polymerase Chain Reaction,
pubmed-meshheading:10631802-Sequence Analysis, DNA,
pubmed-meshheading:10631802-Sequence Homology, Amino Acid
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pubmed:year |
1999
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pubmed:articleTitle |
Characterization and sequencing of glutamine synthetase cDNA from liver of the ureotelic gulf toadfish (Opsanus beta).
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pubmed:affiliation |
Division of Marine Biology and Fisheries, Rosenstiel School of Marine and Atmospheric Science, NIEHS Marine and Freshwater Biomedical Sciences Center, Miami, FL 33149-1098, USA. pwalsh@rsmas.miami.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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