Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley

Manabu Sugimoto; Kazuyoshi Takeda

doi:10.1016/S1381-1177(03)00104-8

Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley

Manabu Sugimoto, Kazuyoshi Takeda

Institute of Plant Science and Resources

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

A cDNA encoding barley phospholipid hydroperoxide glutathione peroxidase (PHGPX)-like protein was cloned and sequenced by the reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends methods. The cDNA comprised 846bp, and included an open reading frame which encodes a polypeptide of 169 amino acid residues with a molecular mass of 18,532Da. The deduced amino acid sequence showed significant identity to plant putative PHGPXs and mammalian PHGPXs. The cloned gene was expressed in Escherichia coli cells to produce an extra protein, which showed a molecular mass similar to the deduced one, and the clone cells were much more tolerant to NaCl stress than the host cells.

Original language	English
Pages (from-to)	397-403
Number of pages	7
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	23
Issue number	2-6
DOIs	https://doi.org/10.1016/S1381-1177(03)00104-8
Publication status	Published - Sep 1 2003

Keywords

Barley
Phospholipid hydroperoxide glutathione peroxidase
Salt stress

ASJC Scopus subject areas

Catalysis
Bioengineering
Biochemistry
Process Chemistry and Technology

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abstract = "A cDNA encoding barley phospholipid hydroperoxide glutathione peroxidase (PHGPX)-like protein was cloned and sequenced by the reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends methods. The cDNA comprised 846bp, and included an open reading frame which encodes a polypeptide of 169 amino acid residues with a molecular mass of 18,532Da. The deduced amino acid sequence showed significant identity to plant putative PHGPXs and mammalian PHGPXs. The cloned gene was expressed in Escherichia coli cells to produce an extra protein, which showed a molecular mass similar to the deduced one, and the clone cells were much more tolerant to NaCl stress than the host cells.",

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AU - Sugimoto, Manabu

AU - Takeda, Kazuyoshi

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AB - A cDNA encoding barley phospholipid hydroperoxide glutathione peroxidase (PHGPX)-like protein was cloned and sequenced by the reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends methods. The cDNA comprised 846bp, and included an open reading frame which encodes a polypeptide of 169 amino acid residues with a molecular mass of 18,532Da. The deduced amino acid sequence showed significant identity to plant putative PHGPXs and mammalian PHGPXs. The cloned gene was expressed in Escherichia coli cells to produce an extra protein, which showed a molecular mass similar to the deduced one, and the clone cells were much more tolerant to NaCl stress than the host cells.

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KW - Phospholipid hydroperoxide glutathione peroxidase

KW - Salt stress

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