Plant Molecular Biology

, Volume 18, Issue 4, pp 691–701 | Cite as

Cloning and sequencing of a cDNA encoding ascorbate peroxidase fromArabidopsis thaliana

  • Akihiro Kubo
  • Hikaru Saji
  • Kiyoshi Tanaka
  • Kunisuke Tanaka
  • Noriaki Kondo
Research Article

Abstract

A cDNA clone encoding ascorbate peroxidase (AP, EC 1.11.1.11) was isolated from a phage λgt11 library of cDNA fromArabidopsis thaliana by immunoscreening with monoclonal antibodies against the enzyme, and then sequenced. The cDNA insert hybridized to a 1.1 kb poly(A)+ RNA from leaves ofA thaliana. Genomic hybridization suggests that the cDNA obtained here corresponds to a single-copy gene. The N-terminal amino acid sequence ofArabidopsis AP was determined by protein sequencing of the immunochemically purified enzyme, and proved to be homologous to the N-terminal amino acid sequence of the chloroplastic AP of spinach. The predicted amino acid sequence of the mature AP ofA. thaliana, deduced from the nucleotide sequence, consists of 249 amino acid residues, which is 34% homologous with cytochromec peroxidase of yeast, but less homologous with other plant peroxidases. Amino acid residues at the active site of yeast cytochromec peroxidase are conserved in the amino acid sequence ofArabidopsis AP. The poly(dG-dT) sequence, which is a potential Z-DNA-forming sequence, was found in the 3′ untranslated region of the cDNA.

Key words

active oxygen Arabidopsis thaliana ascorbate peroxidase cDNA sequence cytochromec peroxidase Z-DNA 

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Copyright information

© Kluwer Academic Publishers 1992

Authors and Affiliations

  • Akihiro Kubo
    • 1
  • Hikaru Saji
    • 2
  • Kiyoshi Tanaka
    • 1
  • Kunisuke Tanaka
    • 3
  • Noriaki Kondo
    • 2
  1. 1.Environmental Biology DivisionNational Institute for Environmental StudiesTsukuba, IbarakiJapan
  2. 2.Regional and Community Environment DivisionNational Institute for Environmental StudiesTsukuba, IbarakiJapan
  3. 3.Faculty of AgricultureKyoto Prefectural UniversityShimogamo, KyotoJapan

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