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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
1998-11-13
|
| pubmed:databankReference | |
| pubmed:abstractText |
Genomic clones for NADH-dependent glutamate synthase (NADH-GOGAT; EC 1.4.1.14) were obtained from a genomic library of rice (Oryza sativa L. cv. Sasanishki). A genomic clone (lambdaOS42, 14 kb) covered an entire structural gene and a 3.7 kb 5'-upstream region from the first methionine. Another clone (lambdaOS23, 14 kb) contained a 2.8 kb 3'-downstream region from the stop codon. A 7047 bp long clone (lambdaOSR51) consisting of full length cDNA for NADH-GOGAT was isolated from a cDNA library prepared using mRNA from roots of rice seedlings treated with 1 mM NH4Cl for 12 h. The presumed transcribed region (11.7 kb) consisted of 23 exons separated by 22 introns. Rice NADH-GOGAT is synthesized as a 2166 amino acid protein with a molecular mass of 236.7 kDa that includes a 99 amino acid presequence. DNA gel blot analysis suggested that NADH-GOGAT occurred as a single gene in rice. Primer extension experiments map the transcription start of NADH-GOGAT to identical positions. The 3. 7 kb 5'-upstream region was able to transiently express a reporter gene in cultured rice cells. Putative motifs related to the regulation of NADH-GOGAT gene expression were looked for within the 5'-upstream region by database.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
8
|
| pubmed:volume |
1387
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
298-308
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9748637-Amino Acid Oxidoreductases,
pubmed-meshheading:9748637-Amino Acid Sequence,
pubmed-meshheading:9748637-Base Sequence,
pubmed-meshheading:9748637-Binding Sites,
pubmed-meshheading:9748637-Cells, Cultured,
pubmed-meshheading:9748637-Cloning, Molecular,
pubmed-meshheading:9748637-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:9748637-Genes, Plant,
pubmed-meshheading:9748637-Genes, Reporter,
pubmed-meshheading:9748637-Glutamate Synthase,
pubmed-meshheading:9748637-Glutamate Synthase (NADH),
pubmed-meshheading:9748637-Molecular Sequence Data,
pubmed-meshheading:9748637-NAD,
pubmed-meshheading:9748637-Oryza sativa,
pubmed-meshheading:9748637-Plant Proteins,
pubmed-meshheading:9748637-RNA, Messenger,
pubmed-meshheading:9748637-Sequence Analysis, DNA,
pubmed-meshheading:9748637-Sequence Homology, Amino Acid,
pubmed-meshheading:9748637-Transfection
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Organization and structure of NADH-dependent glutamate synthase gene from rice plants.
|
| pubmed:affiliation |
Department of Life Science, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai 981-8555, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|