Read/Search this Article
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