A DNA polymerase from the archaeon Sulfolobus solfataricus shows sequence similarity to family B DNA polymerases

• Published in: Nucleic acids research Vol. 20; no. 11; pp. 2711 - 2716
• Main Authors: PISANI, F. M, DE MARTINO, C, ROSSI, M
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 11.06.1992
• Subjects: Amino Acid Sequence; Bacteriology; Base Sequence; Biological and medical sciences; Cloning, Molecular; DNA, Bacterial - genetics; DNA-Directed DNA Polymerase - genetics; Escherichia coli; Fundamental and applied biological sciences. Psychology; Genes, Bacterial; Genetics; Microbiology; Molecular Sequence Data; Restriction Mapping; Sequence Alignment; Sulfolobus - enzymology; Sulfolobus - genetics; Sulfolobus solfataricus; Conserved sequence; DNA polymerase; Nucleotide sequence; Enzyme; Archaeobacteria; Gene product; Sequence alignment; Bacteria; Computer aid; Aminoacid sequence
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/20.11.2711

The gene encoding the thermostable DNA polymerase from the archaeon Sulfolobus solfataricus (strain MT 4) was isolated by means of two degenerate oligonucleotide probes. They were designed on the basis of partial enzyme amino acid sequences. The gene was found to encode a 882 residues polypeptide chain with a deduced molecular mass of about 100 kDa. By comparison with other archaeal genes, putative regulatory sites were identified in the gene-flanking regions. By computer-assisted homology search, several sequence similarities among S. solfataricus and family B DNA polymerases were found. In addition, conserved sequence motifs, implicated in the 3'-5' exonuclease activity of E. coli DNA polymerase I and shared by various family A and B DNA polymerases, were also identified. This result suggests that the proofreading domains of all these enzymes are evolutionarily related.