Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression
| ISSN: |
1617-4623
|
|---|---|
| Keywords: |
Barley ; Embryo ; Aleurone ; Storage globulin ; Gibberellin
|
| Source: |
Springer Online Journal Archives 1860-2000
|
| Topics: |
Biology
|
| Notes: |
Abstract We report identification of a 2189 by 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 637 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. Beg-2 and Beg1 are regulated differently which may indicate variation in storage or utilization properties among the barley globulins.
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798297382419431424 |
|---|---|
| autor | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David |
| autorsonst | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David |
| book_url | http://dx.doi.org/10.1007/BF00281620 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM205446450 |
| issn | 1617-4623 |
| journal_name | Molecular genetics and genomics |
| materialart | 1 |
| notes | Abstract We report identification of a 2189 by 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 637 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. Beg-2 and Beg1 are regulated differently which may indicate variation in storage or utilization properties among the barley globulins. |
| package_name | Springer |
| publikationsjahr_anzeige | 1993 |
| publikationsjahr_facette | 1993 |
| publikationsjahr_intervall | 8009:1990-1994 |
| publikationsjahr_sort | 1993 |
| publisher | Springer |
| reference | 239 (1993), S. 209-218 |
| schlagwort | Barley Embryo Aleurone Storage globulin Gibberellin |
| search_space | articles |
| shingle_author_1 | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David |
| shingle_author_2 | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David |
| shingle_author_3 | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David |
| shingle_author_4 | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David |
| shingle_catch_all_1 | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression Barley Embryo Aleurone Storage globulin Gibberellin Barley Embryo Aleurone Storage globulin Gibberellin Abstract We report identification of a 2189 by 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 637 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. Beg-2 and Beg1 are regulated differently which may indicate variation in storage or utilization properties among the barley globulins. 1617-4623 16174623 Springer |
| shingle_catch_all_2 | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression Barley Embryo Aleurone Storage globulin Gibberellin Barley Embryo Aleurone Storage globulin Gibberellin Abstract We report identification of a 2189 by 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 637 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. Beg-2 and Beg1 are regulated differently which may indicate variation in storage or utilization properties among the barley globulins. 1617-4623 16174623 Springer |
| shingle_catch_all_3 | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression Barley Embryo Aleurone Storage globulin Gibberellin Barley Embryo Aleurone Storage globulin Gibberellin Abstract We report identification of a 2189 by 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 637 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. Beg-2 and Beg1 are regulated differently which may indicate variation in storage or utilization properties among the barley globulins. 1617-4623 16174623 Springer |
| shingle_catch_all_4 | Heck, Gregory R. Chamberlain, Aaron K. Ho, T.-H. David Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression Barley Embryo Aleurone Storage globulin Gibberellin Barley Embryo Aleurone Storage globulin Gibberellin Abstract We report identification of a 2189 by 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 637 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. Beg-2 and Beg1 are regulated differently which may indicate variation in storage or utilization properties among the barley globulins. 1617-4623 16174623 Springer |
| shingle_title_1 | Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression |
| shingle_title_2 | Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression |
| shingle_title_3 | Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression |
| shingle_title_4 | Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Springer Online Journal Archives 1860-2000 |
| timestamp | 2024-05-06T10:07:06.335Z |
| titel | Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression |
| titel_suche | Barley embryo globulin 1 gene, Beg1: Characterization of cDNA, chromosome mapping and regulation of expression |
| topic | W |
| uid | nat_lic_papers_NLM205446450 |