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

Manabu Sugimoto, Kazuyoshi Takeda

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)397-403
Number of pages7
JournalJournal of Molecular Catalysis B: Enzymatic
Volume23
Issue number2-6
DOIs
Publication statusPublished - Sep 1 2003

Fingerprint

phospholipid-hydroperoxide glutathione peroxidase
Phospholipids
Molecular mass
Hordeum
Amino acids
Clone cells
Complementary DNA
Proteins
Polymerase chain reaction
Polypeptides
Transcription
Escherichia coli
Amplification
Amino Acids
Genes
Open Reading Frames
Reverse Transcription
Amino Acid Sequence
Clone Cells
Polymerase Chain Reaction

Keywords

  • Barley
  • Phospholipid hydroperoxide glutathione peroxidase
  • Salt stress

ASJC Scopus subject areas

  • Biochemistry
  • Catalysis
  • Process Chemistry and Technology

Cite this

Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley. / Sugimoto, Manabu; Takeda, Kazuyoshi.

In: Journal of Molecular Catalysis B: Enzymatic, Vol. 23, No. 2-6, 01.09.2003, p. 397-403.

Research output: Contribution to journalArticle

@article{02c5419350994e6381caca103cbc673b,
title = "Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley",
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.",
keywords = "Barley, Phospholipid hydroperoxide glutathione peroxidase, Salt stress",
author = "Manabu Sugimoto and Kazuyoshi Takeda",
year = "2003",
month = "9",
day = "1",
doi = "10.1016/S1381-1177(03)00104-8",
language = "English",
volume = "23",
pages = "397--403",
journal = "Journal of Molecular Catalysis - B Enzymatic",
issn = "1381-1177",
publisher = "Elsevier",
number = "2-6",

}

TY - JOUR

T1 - Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley

AU - Sugimoto, Manabu

AU - Takeda, Kazuyoshi

PY - 2003/9/1

Y1 - 2003/9/1

N2 - 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.

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.

KW - Barley

KW - Phospholipid hydroperoxide glutathione peroxidase

KW - Salt stress

UR - http://www.scopus.com/inward/record.url?scp=0041932459&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0041932459&partnerID=8YFLogxK

U2 - 10.1016/S1381-1177(03)00104-8

DO - 10.1016/S1381-1177(03)00104-8

M3 - Article

AN - SCOPUS:0041932459

VL - 23

SP - 397

EP - 403

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

SN - 1381-1177

IS - 2-6

ER -