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Characterization of a Novel 4.0-kb Y-type HMW-GS from Eremopyrum distans.

Authors :
DAI, S. F.
XU, D. Y.
WEN, Z. J.
SONG, Z. P.
CHEN, H. X.
LI, H. Y.
LI, J. R.
KANG, L. Z.
YAN, Z. H.
Source :
Cereal Research Communications; 2018, Vol. 46 Issue 3, p499-509, 11p
Publication Year :
2018

Abstract

A novel 4.0-kb Fy was sequenced and bacterially expressed. This gene, the largest y-type HMW-GS currently reported, is 4,032-bp long and encodes a mature protein with 1,321 amino acid (AA) residues. The 4.0-kb Fy shows novel modifications in all domains. In the N-terminal, it contains only 67 AA residues, as three short peptides are absent. In the repetitive domain, the undecapeptide RYYPSVTSPQQ is completely lost and the dodecapeptide GSYYPGQTSPQQ is partially absent. A novel motif unit, PGQQ, is present in addition to the two standard motif units PGQGQQ and GYYPTSPQQ. Besides, an extra cysteine residue also occurs in the middle of this domain. The large molecular mass of the 4.0-kb Fy is mainly due to the presence of an extra-long repetitive domain with 1,279 AA residues. The novel 4.0-kb Fy gene is of interest in HMW-GS gene evolution as well as to wheat quality improvement with regard to its longest repetitive domain length and extra cysteines residues. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
01333720
Volume :
46
Issue :
3
Database :
Complementary Index
Journal :
Cereal Research Communications
Publication Type :
Academic Journal
Accession number :
131414827
Full Text :
https://doi.org/10.1556/0806.46.2018.018