cDNA Cloning and Analysis of the Chicken Homolog of E.coli Endonuclease Ⅲ cDNA Cloning and Analysis of the Chicken Homolog of E. coli Endonuclease III

    • Seki Shuji
    • Department of Human Nutrition, Faculty of Contemporary Life Science, Chugokugakuen University
    • Sarker Altaf H.
    • Department of Cellular and Molecular Biology, Life Science Division, Lawrence Berkeley National Laboratory, University of California
    • Nakamura Takashi
    • Department of Molecular Biology, Okayama University Graduate School of Medicine and Dentistry
    • Seki Yuichi
    • Tsuyama Medical Examination Center of Chugoku Occupational Health Association

    • Ikeda Shogo
    • Department of Biological Chemistry, Okayama University of Science

Abstract

We have cloned and analyzed the cDNA for the chicken homolog of E. coli endonuclease Ⅲ (chNthll; chicken homolog of E. coli endonuclease Ⅲ-like 1). The cDNA was isolated from a chicken embryonic cDNA library using cDNA of mouse endonuclease Ⅲ (mNthll) as a probe. The obtained cDNA was 1211 nucleotide long encoding a protein consisting of 281 amino acids with a predicted molecular mass of 32 kDa. The amino acid sequence exhibits 66% and 67%homologies with those of the human and mouse homologs, respectively, and the homologies are mostly concentrated within the C-terminal, 2/3 region of the sequence. The two motifs consisting of a helix-hairpin-helix and an iron-sulphur [4Fe-4S] cluster were also preserved in the chicken homolog suggesting similar enzymatic function in chicken cells as that of endonuclease Ⅲ in E. coli.

We have cloned and analyzed the cDNA for the chicken homolog of E. coli endonuclease III (chNthll ; chicken homolog of E. coli endonuclease III-like 1). The cDNA was isolated from a chicken embryonic cDNA library using cDNA of mouse endonuclease III (mNthll) as a probe. The obtained cDNA was 1211 nucleotide long encoding a protein consisting of 281 amino acids with a predicted molecular mass of 32 kDa. The amino acid sequence exhibits 66% and 67% homologies with those of the human and mouse homologs, respectively, and the homologies are mostly concentrated within the C-terminal, 2/3 region of the sequence. The two motifs consisting of a helix-hairpin-helix and an iron-sulphur [4Fe-4S] cluster were also preserved in the chicken homolog suggesting similar enzymatic function in chicken cells as that of endonuclease III in E. coli.

Journal

Chugokugakuen journal   [List of Volumes]

Chugokugakuen journal 5, 23-27, 2006  [Table of Contents]

Chugokugakuen University

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Codes

  • NII Article ID (NAID) :
    110006426551
  • NII NACSIS-CAT ID (NCID) :
    AA11806612
  • Text Lang :
    ENG
  • Article Type :
    Departmental Bulletin Paper
  • ISSN :
    13481452
  • Databases :
    NII-ELS  IR