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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1993-9-24
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pubmed:abstractText |
Genes encoding the beta-conglycinin seed storage proteins of soybean are expressed only in seeds during specific stages of development. The different subunits of beta-conglycinin, alpha', alpha and beta, are encoded by distinct members of a gene family. Yet there are marked differences in the regulation of the genes encoding the alpha'/alpha and beta subunits. Previous work (Chen et al., EMBO J 7: 297-302, 1988) identified a seed specific transcriptional enhancer upstream of a gene encoding the alpha' subunit. Mutations were made within this region to discern its functional components. Among those identified is a 62 bp region (between -77 and -140) that contains a vicilin box consensus sequence as well as a sequence that binds the soybean nuclear factor SEF4 in vitro. A second region, which contains a sequence homologous to the core of the legumin box consensus (i.e., CATGCAT-like or RY repeat element) at -246, was also shown to affect the activity of this enhancer in transgenic plants. A series of 5' terminal deletions were used to identify regulatory elements upstream of the beta subunit gene. Two regions were identified (from -553 to -442 and from -308 to -72) that, when deleted, led to a marked reduction in gene expression. Both of these elements contain sequences that bind SEF4 in vitro. The distal element also contains an AT-rich segment that recognizes a second nuclear factor, SEF1, in vitro. Neither of these elements contains any homology to the vicilin box consensus.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Globulins,
http://linkedlifedata.com/resource/pubmed/chemical/Seed Storage Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Soybean Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-conglycinin protein, Glycine...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0167-4412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
873-85
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8358033-Antigens, Plant,
pubmed-meshheading:8358033-Base Sequence,
pubmed-meshheading:8358033-Cloning, Molecular,
pubmed-meshheading:8358033-DNA,
pubmed-meshheading:8358033-Enhancer Elements, Genetic,
pubmed-meshheading:8358033-Gene Expression Regulation,
pubmed-meshheading:8358033-Globulins,
pubmed-meshheading:8358033-Kinetics,
pubmed-meshheading:8358033-Molecular Sequence Data,
pubmed-meshheading:8358033-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:8358033-Restriction Mapping,
pubmed-meshheading:8358033-Seed Storage Proteins,
pubmed-meshheading:8358033-Seeds,
pubmed-meshheading:8358033-Sequence Deletion,
pubmed-meshheading:8358033-Soybean Proteins,
pubmed-meshheading:8358033-Soybeans
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pubmed:year |
1993
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pubmed:articleTitle |
Upstream regulatory sequences from two beta-conglycinin genes.
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pubmed:affiliation |
Department of Biology, Washington University, St. Louis, MO 63130.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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