Molecular characterization of a novel HMW glutenin subunit Dx2.3*t from Aegilops tauschii

B. Feng; Z.B. Xu; X. Wang; F. Jiang; G.J. Zhao; C. Xiang; T. Wang

doi:10.1556/crc.2013.0071

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Cereal Research Communications

Volume/Issue:: Volume 42: Issue 3

Molecular characterization of a novel HMW glutenin subunit Dx2.3*^t from Aegilops tauschii

Authors:

B. Feng

B. Feng Chinese Academy of Sciences Chengdu Institute of Biology Chengdu 610041 China

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Z.B. Xu

Z.B. Xu Chinese Academy of Sciences Chengdu Institute of Biology Chengdu 610041 China

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X. Wang

X. Wang Chinese Academy of Sciences Chengdu Institute of Biology Chengdu 610041 China

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F. Jiang

F. Jiang

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G.J. Zhao

G.J. Zhao

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C. Xiang

C. Xiang

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T. Wang

T. Wang Chinese Academy of Sciences Chengdu Institute of Biology Chengdu 610041 China

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Pages:: 503–513

Online Publication Date:: 21 Feb 2014

Publication Date:: 01 Sep 2014

Article Category:: Research Article

DOI:: https://doi.org/10.1556/crc.2013.0071

Keywords:: Aegilops tauschii ; HMW glutenin subunit; 1Dx2.3*t; phylogenetic analysis

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High molecular weight (HMW) glutenin subunits are important seed storage proteins in wheat and its related species. Novel HMWglutenin 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 identical 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.

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Cereal Research Communications A Quarterly of the Cereal Research Non-Profit Ltd. Company

Print ISSN:: 0133-3720

Online ISSN:: 1788-9170

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Cereal Research Communications
Language	English
Size	A4
Year of Foundation	1973
Volumes per Year	1
Issues per Year	4
Founder	Akadémiai Kiadó
Founder's Address	H-1117 Budapest, Hungary 1516 Budapest, PO Box 245
Publisher	Akadémiai Kiadó Springer Nature Switzerland AG
Publisher's Address	H-1117 Budapest, Hungary 1516 Budapest, PO Box 245. CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible Publisher	Chief Executive Officer, Akadémiai Kiadó
ISSN	0133-3720 (Print)
ISSN	1788-9170 (Online)