Molecular cloning, sequencing analysis and expression of the catalase-peroxidase gene from Halobacterium salinarum.
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.
Long
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Department of Biochemistry and Molecular Biology, Mississippi State University, Mississippi State, MS 39762, USA.
Salin
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ML
D000595:Amino Acid Sequence; D001483:Base Sequence; D002374:Catalase / Q000235:genetics*; D003001:Cloning, Molecular; D019641:DNA, Archaeal / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D019766:Genes, Archaeal; D019617:Halobacterium salinarum / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D009195:Peroxidase / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D019641:DNA, Archaeal; D011993:Recombinant Fusion Proteins; D002374:Catalase; D009195:Peroxidase