Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases: similarity to adenine and cytosine-C5 DNA-methylases
Open Access
- 11 December 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 17 (23) , 9823-9832
- https://doi.org/10.1093/nar/17.23.9823
Abstract
The sequences coding for DNA[cytosine-N4]methyltransferases MvaI (from Micrococcus varians RFL19) and Cfr9I (from Citrobacter freundii RFL9) have been determined. The predicted methylases are proteins of 454 and 300 amino acids, respectively. Primary structure comparison of M.Cfr9I and another m4C-foming methylase, M.Pvu II, revealed extended regions of homology. The sequence comparison of the three DNA[cytosine-N4]-methylases using originally developed software revealed two conserved patterns, DPF-GSGT and TSPPY, which were found similar also to those of adenine and DNA[cytosine-C5]-methylases These data provided a basis for global alignment and classification of DNA-methylase sequences. Structural considerations led us to suggest that the first region could be the binding site of AdoMet, while the second is thought to be directly involved in the modification of the exocyclic amino group.Keywords
This publication has 46 references indexed in Scilit:
- Cloning and characterization of the genes encoding theMspl restriction modification systemNucleic Acids Research, 1989
- Sequence, internal homology and high-level expression of the gene for a DNA-(cytosineN4)-methyltransferase, M-PvuIINucleic Acids Research, 1989
- N4-methylcytosine as a minor base in bacterial DNAJournal of Bacteriology, 1987
- Nucleotide sequence and expression of the gene encoding theEcoRII modification enzymeNucleic Acids Research, 1987
- DNA methyltransferase genes of Bacillus subtilis phages: comparison of their nucleotide sequencesGene, 1986
- Nucleotide sequence of thePaeR7 restriction/modification system and partial characterization of its protein productsNucleic Acids Research, 1985
- Nucleotide sequence of the Dpn II DNA methylase gene of Streptococcus pneumoniae and its relationship to the dam gene of Escherichia coli.Proceedings of the National Academy of Sciences, 1985
- Rapid and Sensitive Protein Similarity SearchesScience, 1985
- Investigation of restriction-modification enzymes fromM. variansRFL19 with a new type of specificity toward modification of substrateNucleic Acids Research, 1985
- DNA methylation in thermophilic bacteria: N4-methylcytosine, 5-methylcytosine, and N5methyladenineNucleic Acids Research, 1985