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    DNA Seq. 2001 Jul;12(1):39-51.

    Molecular cloning, sequencing analysis and expression of the catalase-peroxidase gene from Halobacterium salinarum.

    Long S, Salin ML.

    Department of Biochemistry and Molecular Biology, Mississippi State University, Mississippi State, MS 39762, USA.

    The gene encoding catalase-peroxidase was cloned from chromosomal DNA from the Archaea, Halobacterium salinarum. The nucleotide sequence of a 3.5 kb fragment, containing the catalase-peroxidase gene and its flanking regions was determined. A 2.16 kb open reading frame was obtained, encoding the enzyme which was comprised of 720 amino acid residues with a calculated molecular weight of 80 kDa. The deduced amino acid sequence of the H. salinarum catalase-peroxidase showed a high degree of identity to other bifunctional catalase-peroxidases. A transcriptional start site was identified 183 bp upstream of the translational start codon. Southern blot analysis indicated that catalase-peroxidase was a single copy gene. The Archaeal catalase-peroxidase gene was expressed in Escherichia coli, and the expressed fusion protein exhibited both catalase and peroxidase activities.

    PMID: 11702717 [PubMed - indexed for MEDLINE]

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