Authors:
L.J. Wu Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, China
University of Chinese Academy of Sciences, Beijing 100049, China

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Y. Shang Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, China
University of Chinese Academy of Sciences, Beijing 100049, China

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T. Liu Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, China
University of Chinese Academy of Sciences, Beijing 100049, China

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W.J. Chen Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, China
Qinghai Province Key Laboratory of Crop Molecular Breeding, Xining 810008, China

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B.L. Liu Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, China
Qinghai Province Key Laboratory of Crop Molecular Breeding, Xining 810008, China

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L.Q. Zhang Triticeae Research Institute, Sichuan Agricultural University, Chengdu 611130, China

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D.C. Liu Triticeae Research Institute, Sichuan Agricultural University, Chengdu 611130, China

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B. Zhang Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, China
Qinghai Province Key Laboratory of Crop Molecular Breeding, Xining 810008, China

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H.G. Zhang Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, China
Qinghai Province Key Laboratory of Crop Molecular Breeding, Xining 810008, China

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In this study, the cDNA of homocysteine S-methyltransferase was isolated from Aegilops tauschii Coss., with the gene accordingly designated as AetHMT1. Similar to other methyltransferases, AetHMT1 contains a GGCCR consensus sequence for a possible zinc-binding motif near the C-terminal and a conserved cysteine residue upstream of the zinc-binding motif. Analysis of AetHMT1 uncovered no obvious chloroplast or mitochondrial targeting sequences. We functionally expressed AetHMT1 in Escherichia coli and confirmed its biological activity, as evidenced by a positive HMT enzyme activity of 164.516 ± 17.378 nmol min−1 mg−1 protein when catalyzing the transformation of L-homocysteine. Compared with the bacterium containing the empty vector, E. coli harboring the recombinant AetHMT1 plasmid showed much higher tolerance to selenate and selenite. AetHMT1 transcript amounts in different organs were increased by Na2SeO4 treatment, with roots accumulating higher amounts than stems, old leaves and new leaves. We have therefore successfully isolated HMT1 from Ae. tauschii and characterized the biochemical and physiological functions of the corresponding protein.

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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)