M.ø3TII: a new monospecific DNA (cytosine-C5) methyltransferase with pronounced amino acid sequence similarity to a family of adenine-N6-DNA-methyltransferases
| Autor: | Sunghee Chai, Peter-Andreas Terschüren, Jörn Walter, Mario Noyer-Weidner, Thomas A. Trautner |
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| Rok vydání: | 1994 |
| Předmět: |
Site-Specific DNA-Methyltransferase (Adenine-Specific)
Genes Viral Sequence analysis Molecular Sequence Data Restriction Mapping Sequence alignment Bacillus Phages Biology Methylation Substrate Specificity Conserved sequence Viral Proteins chemistry.chemical_compound Restriction map Genetics Amino Acid Sequence DNA (Cytosine-5-)-Methyltransferases RNA Messenger Gene Peptide sequence Conserved Sequence Viral Structural Proteins chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid Sequence Analysis DNA Amino acid Biochemistry chemistry DNA Viral RNA Viral Sequence Alignment DNA Bacillus subtilis |
| Zdroj: | Nucleic Acids Research. 22:5517-5723 |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | The temperate B.subtilis phages phi 3T and rho 11s code, in addition to the multispecific DNA (cytosine-C5) methyltransferases (C5-MTases) M. phi 3TI and M. rho 11sI, which were previously characterized, for the identical monospecific C5-MTases M. phi 3TII and M. rho 11sII. These enzymes modify the C of TCGA sites, a novel target specificity among C5-MTases. The primary sequence of M. phi 3TII (326 amino acids) shows all conserved motifs typical of the building plan of C5-MTases. The degree of relatedness between M. phi 3TII and all other mono- or multispecific C5-MTases ranges from 30-40% amino acid identity. Particularly M. phi 3TII does not show pronounced similarity to M. phi 3TI indicating that both MTase genes were not generated from one another but were acquired independently by the phage. The amino terminal part of the M. phi 3TII (preceding the variable region 'V'), which predominantly constitutes the catalytic domain of the enzyme, exhibits pronounced sequence similarity to the amino termini of a family of A-N6-MTases, which--like M.TaqI--recognize the general sequence TNNA. This suggests that recently described similarities in the general three dimensional organization of C5- and A-N6-MTases imply divergent evolution of these enzymes originating from a common molecular ancestor. |
| Databáze: | OpenAIRE |
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