title: Similarity relations of DNA and RNA polymerases investigated by the principal component analysis of amino acid sequences.
abstract: The principal component analysis based on the physicochemical properties of amino acid residues is applied to DNA and RNA polymerases to assign the sequence motifs for the polymerization activities of these proteins. After the reconfirmation of the sequence motifs of families A and B of DNA polymerases indicated previously, it elucidates the sequence motifs for the polymerization activity of DNA polymerase III (family C) by the similarity to the polymerization center of multimeric DNA dependent RNA polymerases. This identification proceeds to clarify the sequence motifs for polymerization activities of primases; eukaryotic and archaebacterial primases carry motifs similar to those of family C, while the motifs of eubacterial primase fall into the category of the motifs in family B DNA polymerases such as alpha, delta, epsilon and II. This finding means that DNA dependent RNA polymerases are also divided into groups corresponding to three families, A, B and C, because the monomeric DNA dependent RNA polymerases in phages are reconfirmed to carry sequence motifs similar to those of family A DNA polymerases. Furthermore, the three families of polymerization motifs are found to fall within the variation range of polymerization motifs displayed by many RNA dependent RNA polymerases, suggesting a close evolutionary relation between them. The sequence motifs for polymerization activities of reverse transcriptase and telomerase seem to be the intermediate between family A DNA polymerase and some RNA dependent RNA polymerases, e.g., from Leviviridae. On the contrary, the sequence fragments similar to the nucleotidyltransferase superfamily including DNA polymerase beta are not found in any RNA dependent RNA polymerase, suggesting their other lineage of polymerization motifs.
authors.affiliation: Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, Noda, Japan. jotsuka@rs. noda.sut.ac.jp
authors.forename: J
authors.initials: J
authors.lastname: Otsuka
authors.forename: N
authors.initials: N
authors.lastname: Kikuchi
authors.forename: S
authors.initials: S
authors.lastname: Kojima
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D001412:Bacillus subtilis; D001435:Bacteriophages; D004258:DNA Polymerase III / Q000737:chemistry; D019915:DNA Primase / Q000737:chemistry; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry*; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry*; D004926:Escherichia coli; D005051:Eubacterium; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D012194:RNA-Directed DNA Polymerase / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012984:Software; D019098:Telomerase / Q000737:chemistry
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D019915:DNA Primase; D012194:RNA-Directed DNA Polymerase; D019098:Telomerase; D012321:DNA-Directed RNA Polymerases; D004258:DNA Polymerase III; D004259:DNA-Directed DNA Polymerase