ArticleMolecular & general genetics : MGG1993
Barley embryo globulin 1 gene, Beg1: characterization of cDNA, chromosome mapping and regulation of expression.
Article in Molecular & general genetics : MGG, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 47 citations in OpenAlex.
- Comparative Proteomic Analysis of Two Barley Cultivars (Hordeum vulgare L.) with Contrasting Grain Protein Content.Frontiers in plant science · 2016Article
- Article
- Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos.BMC research notes · 2012Article
- Endosperm development in Brachypodium distachyon.Journal of experimental botany · 2011Article
- Brachypodium distachyon grain: identification and subcellular localization of storage proteins.Journal of experimental botany · 2010Article
- Identification of three wheat globulin genes by screening a Triticum aestivum BAC genomic library with cDNA from a diabetes-associated globulin.BMC plant biology · 2009Article
- Genetic manipulation of lysine catabolism in maize kernels.Plant molecular biology · 2009Article
- Protein sorting and expression of a unique soybean cotyledon protein, GmSBP, destined for the protein storage vacuole.Plant molecular biology · 2003Article
- Degradation of oat mRNAs during seed development.Plant molecular biology · 1999Article
- Speciation and domestication in maize and its wild relatives: evidence from the globulin-1 gene.Genetics · 1998Article
- Gibberellin-repressible gene expression in the barley aleurone layer.Plant molecular biology · 1996Article
- Article
- Transient expression of a lysine-rich vicilin gene ofVicia faba in barley endosperm detected by immunological tissue printing after particle bombardment.Plant cell reports · 1995Article
- Gibberellins: perception, transduction and responses.Plant molecular biology · 1994Review
- Tissue-specific expression of an oat 12S seed globulin gene in developing tobacco seeds: differential mRNA and protein accumulation.Plant molecular biology · 1994Article
- The expression of serine carboxypeptidases during maturation and germination of the barley grain.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report identification of a 2189 bp cDNA clone from barley corresponding to a single-copy gene, Beg1 (Barley embryo globulin), on chromosome 4, which encodes a storage globulin. In barley, the major protein reserve in the aleurone layer belongs to the 7S globulin class of proteins found in many seeds. Electrophoretically and antigenically similar proteins are present in the barley embryo. Accumulation of Beg1 mRNA was noted beginning 15-20 days post-anthesis in both the aleurone layer and embryo of the developing barley grain but not in the starchy endosperm. A high level of Beg1 mRNA is also present in the mature imbibed aleurones, which can be repressed by treatment with gibberellic acid. This repressive effect of gibberellin on the levels of Beg1 mRNA is confirmed in the gibberellin response-constitutive mutant, slender, whose aleurone layers do not accumulate Beg1 mRNA even in the absence of applied gibberellic acid. The deduced primary translation product of the Beg1 mRNA is a 63.7 amino acid (72 kDa) protein with homology to maize embryo globulin 1 (GLB1) and a partial sequence of a wheat 7S globulin. The internal amino acid sequence of BEG1 closely matches the N-terminal sequence of isolated barley aleurone globulin. Seven imperfect tandem repeats of 16 amino acids each are present near the N-terminus of BEG1, which conform to the consensus HGEGEREEEXGRGRGR, and contribute to the observed unusual amino acid composition of this protein. A second, distinct barley globulin gene, Beg2, which is homologous to maize Glb2, was detected by Northern and Southern analysis. Beg2 and Beg1 are regulated differently which may indicate variation in storage or utilization properties among the barley globulins.
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