Molecular Characterization of a Novel HMW Glutenin Subunit Dx2.3ᵗ from Aegilops tauschii
High molecular weight (HMW) glutenin subunits are important seed storage proteins in wheat and its related species. Novel HMW glutenin subunits in Aegilops tauschii accession of TA2484 were detected and characterized. SDS-PAGE analysis revealed the y-type subunit from TA2484 displayed similar electr...
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| Veröffentlicht in: | Cereal research communications 2014-09, Vol.42 (3), p.503-513 |
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| creator | Feng, B. Xu, Z.B. Wang, X. Jiang, F. Zhao, G.J. Xiang, C. Wang, T. |
| description | High molecular weight (HMW) glutenin subunits are important seed storage proteins in wheat and its related species. Novel HMW glutenin subunits in Aegilops tauschii accession of TA2484 were detected and characterized. SDS-PAGE analysis revealed the y-type subunit from TA2484 displayed similar electrophoretic mobility compared to that of 1Dy12 subunit. However, the electrophoretic mobility of x-type subunit was faster than that of 1Dx2 subunit. The primary structure of the two cloned subunits from TA2484 was similar to that of the x- and y-type subunits reported before. However, the 148 residues of the x-type subunit, which contained the sequence element GHCPTSLQQ, in the middle of the repetitive domain was quite different from other x-type subunits. Moreover, the 68 residues in this region were idential to those of the y-type subunits from the same accession. Consequently, 1Dx2.3*ᵗ (x-type subunit of TA2484) contains an extra cystenin residue located at the repetitive domain, which is novel compared to the x-type subunits reported so far. Phylogenetic analysis indicated that two subunits from accession TA2484 were in the x- and y-type subunit cluster, but bootstrapping value of 100% gave high support for the spilt between two subunits (1Dx2.3*ᵗ and 1Dy12.3*ᵗ) and their alleles, respectively. A hypothesis on the genetic mechanism generating this novel sequence of 1Dx2.3*ᵗ subunit is suggested. |
| doi_str_mv | 10.1556/CRC.2013.0071 |
| format | Article |
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Novel HMW glutenin subunits in Aegilops tauschii accession of TA2484 were detected and characterized. SDS-PAGE analysis revealed the y-type subunit from TA2484 displayed similar electrophoretic mobility compared to that of 1Dy12 subunit. However, the electrophoretic mobility of x-type subunit was faster than that of 1Dx2 subunit. The primary structure of the two cloned subunits from TA2484 was similar to that of the x- and y-type subunits reported before. However, the 148 residues of the x-type subunit, which contained the sequence element GHCPTSLQQ, in the middle of the repetitive domain was quite different from other x-type subunits. Moreover, the 68 residues in this region were idential to those of the y-type subunits from the same accession. Consequently, 1Dx2.3*ᵗ (x-type subunit of TA2484) contains an extra cystenin residue located at the repetitive domain, which is novel compared to the x-type subunits reported so far. Phylogenetic analysis indicated that two subunits from accession TA2484 were in the x- and y-type subunit cluster, but bootstrapping value of 100% gave high support for the spilt between two subunits (1Dx2.3*ᵗ and 1Dy12.3*ᵗ) and their alleles, respectively. A hypothesis on the genetic mechanism generating this novel sequence of 1Dx2.3*ᵗ subunit is suggested.</description><identifier>ISSN: 0133-3720</identifier><identifier>EISSN: 1788-9170</identifier><identifier>DOI: 10.1556/CRC.2013.0071</identifier><language>eng</language><publisher>Cham: AKADÉMIAI KIADÓ</publisher><subject>Agriculture ; Amino acids ; Genetic loci ; Genetic variation ; Hexaploidy ; Life Sciences ; Literary characterization ; Molecular weight ; Open reading frames ; Phylogenetics ; Plant Breeding/Biotechnology ; Plant Genetics and Genomics ; Plant Physiology ; Proteins ; Quality and Utilization ; Wheat flour</subject><ispartof>Cereal research communications, 2014-09, Vol.42 (3), p.503-513</ispartof><rights>Akadémiai Kiadó 2014</rights><rights>Akadémiai Kiadó, Budapest 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-j611-623b78a9791f575ff4c3acc00f3931a1292c554bca076b9cb5893753f9efa7aa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/24689423$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/24689423$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,777,781,800,27905,27906,41469,42538,51300,57998,58231</link.rule.ids></links><search><creatorcontrib>Feng, B.</creatorcontrib><creatorcontrib>Xu, Z.B.</creatorcontrib><creatorcontrib>Wang, X.</creatorcontrib><creatorcontrib>Jiang, F.</creatorcontrib><creatorcontrib>Zhao, G.J.</creatorcontrib><creatorcontrib>Xiang, C.</creatorcontrib><creatorcontrib>Wang, T.</creatorcontrib><title>Molecular Characterization of a Novel HMW Glutenin Subunit Dx2.3ᵗ from Aegilops tauschii</title><title>Cereal research communications</title><addtitle>CEREAL RESEARCH COMMUNICATIONS</addtitle><description>High molecular weight (HMW) glutenin subunits are important seed storage proteins in wheat and its related species. Novel HMW glutenin subunits in Aegilops tauschii accession of TA2484 were detected and characterized. SDS-PAGE analysis revealed the y-type subunit from TA2484 displayed similar electrophoretic mobility compared to that of 1Dy12 subunit. However, the electrophoretic mobility of x-type subunit was faster than that of 1Dx2 subunit. The primary structure of the two cloned subunits from TA2484 was similar to that of the x- and y-type subunits reported before. However, the 148 residues of the x-type subunit, which contained the sequence element GHCPTSLQQ, in the middle of the repetitive domain was quite different from other x-type subunits. Moreover, the 68 residues in this region were idential to those of the y-type subunits from the same accession. Consequently, 1Dx2.3*ᵗ (x-type subunit of TA2484) contains an extra cystenin residue located at the repetitive domain, which is novel compared to the x-type subunits reported so far. Phylogenetic analysis indicated that two subunits from accession TA2484 were in the x- and y-type subunit cluster, but bootstrapping value of 100% gave high support for the spilt between two subunits (1Dx2.3*ᵗ and 1Dy12.3*ᵗ) and their alleles, respectively. A hypothesis on the genetic mechanism generating this novel sequence of 1Dx2.3*ᵗ subunit is suggested.</description><subject>Agriculture</subject><subject>Amino acids</subject><subject>Genetic loci</subject><subject>Genetic variation</subject><subject>Hexaploidy</subject><subject>Life Sciences</subject><subject>Literary characterization</subject><subject>Molecular weight</subject><subject>Open reading frames</subject><subject>Phylogenetics</subject><subject>Plant Breeding/Biotechnology</subject><subject>Plant Genetics and Genomics</subject><subject>Plant Physiology</subject><subject>Proteins</subject><subject>Quality and Utilization</subject><subject>Wheat flour</subject><issn>0133-3720</issn><issn>1788-9170</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><recordid>eNotkN9KwzAchYMoOKeXXgp5gdb8aZrmclTdhE1BB4I34deQbCldM9JW1BfxSXwg38QOvTpw4DsHPoQuKUmpEPl1-VSmjFCeEiLpEZpQWRSJopIco8lY84RLRk7RWdfVhIhMqWyCXlehsWZoIOJyCxFMb6P_hN6HFgeHAT-EN9vgxeoFz5uht61v8fNQDa3v8c07S_nP9xd2MezwzG58E_Yd7mHozNb7c3TioOnsxX9O0frudl0ukuXj_L6cLZM6pzTJGa9kAUoq6oQUzmWGgzGEOK44BcoUM0JklQEi80qZShSKS8Gdsg4kAJ-i9G-220ffbmzUdRhiOz5qSvRBjB7F6IMYfRAzAld_QN31IeqR2kH80CzLC5Uxzn8BgKFgbg</recordid><startdate>20140901</startdate><enddate>20140901</enddate><creator>Feng, B.</creator><creator>Xu, Z.B.</creator><creator>Wang, X.</creator><creator>Jiang, F.</creator><creator>Zhao, G.J.</creator><creator>Xiang, C.</creator><creator>Wang, T.</creator><general>AKADÉMIAI KIADÓ</general><general>Springer International Publishing</general><scope>C6C</scope></search><sort><creationdate>20140901</creationdate><title>Molecular Characterization of a Novel HMW Glutenin Subunit Dx2.3ᵗ from Aegilops tauschii</title><author>Feng, B. ; Xu, Z.B. ; Wang, X. ; Jiang, F. ; Zhao, G.J. ; Xiang, C. ; Wang, T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j611-623b78a9791f575ff4c3acc00f3931a1292c554bca076b9cb5893753f9efa7aa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Agriculture</topic><topic>Amino acids</topic><topic>Genetic loci</topic><topic>Genetic variation</topic><topic>Hexaploidy</topic><topic>Life Sciences</topic><topic>Literary characterization</topic><topic>Molecular weight</topic><topic>Open reading frames</topic><topic>Phylogenetics</topic><topic>Plant Breeding/Biotechnology</topic><topic>Plant Genetics and Genomics</topic><topic>Plant Physiology</topic><topic>Proteins</topic><topic>Quality and Utilization</topic><topic>Wheat flour</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Feng, B.</creatorcontrib><creatorcontrib>Xu, Z.B.</creatorcontrib><creatorcontrib>Wang, X.</creatorcontrib><creatorcontrib>Jiang, F.</creatorcontrib><creatorcontrib>Zhao, G.J.</creatorcontrib><creatorcontrib>Xiang, C.</creatorcontrib><creatorcontrib>Wang, T.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><jtitle>Cereal research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Feng, B.</au><au>Xu, Z.B.</au><au>Wang, X.</au><au>Jiang, F.</au><au>Zhao, G.J.</au><au>Xiang, C.</au><au>Wang, T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Characterization of a Novel HMW Glutenin Subunit Dx2.3ᵗ from Aegilops tauschii</atitle><jtitle>Cereal research communications</jtitle><stitle>CEREAL RESEARCH COMMUNICATIONS</stitle><date>2014-09-01</date><risdate>2014</risdate><volume>42</volume><issue>3</issue><spage>503</spage><epage>513</epage><pages>503-513</pages><issn>0133-3720</issn><eissn>1788-9170</eissn><abstract>High molecular weight (HMW) glutenin subunits are important seed storage proteins in wheat and its related species. Novel HMW glutenin subunits in Aegilops tauschii accession of TA2484 were detected and characterized. SDS-PAGE analysis revealed the y-type subunit from TA2484 displayed similar electrophoretic mobility compared to that of 1Dy12 subunit. However, the electrophoretic mobility of x-type subunit was faster than that of 1Dx2 subunit. The primary structure of the two cloned subunits from TA2484 was similar to that of the x- and y-type subunits reported before. However, the 148 residues of the x-type subunit, which contained the sequence element GHCPTSLQQ, in the middle of the repetitive domain was quite different from other x-type subunits. Moreover, the 68 residues in this region were idential to those of the y-type subunits from the same accession. Consequently, 1Dx2.3*ᵗ (x-type subunit of TA2484) contains an extra cystenin residue located at the repetitive domain, which is novel compared to the x-type subunits reported so far. Phylogenetic analysis indicated that two subunits from accession TA2484 were in the x- and y-type subunit cluster, but bootstrapping value of 100% gave high support for the spilt between two subunits (1Dx2.3*ᵗ and 1Dy12.3*ᵗ) and their alleles, respectively. A hypothesis on the genetic mechanism generating this novel sequence of 1Dx2.3*ᵗ subunit is suggested.</abstract><cop>Cham</cop><pub>AKADÉMIAI KIADÓ</pub><doi>10.1556/CRC.2013.0071</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Agriculture Amino acids Genetic loci Genetic variation Hexaploidy Life Sciences Literary characterization Molecular weight Open reading frames Phylogenetics Plant Breeding/Biotechnology Plant Genetics and Genomics Plant Physiology Proteins Quality and Utilization Wheat flour |
| title | Molecular Characterization of a Novel HMW Glutenin Subunit Dx2.3ᵗ from Aegilops tauschii |
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