Sequence-specific BamHI methylase. Purification and characterization.

  title={Sequence-specific BamHI methylase. Purification and characterization.},
  author={Glenn A. Nardone and J George and J. G. Chirikjian},
  journal={The Journal of biological chemistry},
  volume={259 16},
BamHI methylase has been purified to apparent homogeneity. The isolated form of the enzyme is a single polypeptide with a molecular weight of 56,000 as determined by sodium dodecyl sulfate-polyacrylamide electrophoresis. Unlike BamHI endonuclease, which is isolated as a dimer and higher aggregates, the methylase has no apparent higher form. The methylase requires S-adenosyl-L-methionine as the methyl-group donor and is inhibited by Mg2+. The enzyme is also inhibited by 2,3-butanedione and… Expand
Purification and biochemical characterization of the EcaI DNA methyltransferase.
The EcaI GGTNACC-specific DNA-adenine modification methyltransferase has been purified to apparent homogeneity and the S-adenosylmethionine analog sinefungin was shown to be a very strong inhibitor of the DNA methyl transferase reaction. Expand
Crystal structure of MboIIA methyltransferase.
The overall structure of the enzyme closely resembles that of M.RsrI, however, the cofactor-binding pocket in M.MboIIA forms a closed structure which is in contrast to the open-form structures of other known MTases. Expand
Biochemical and structural characterization of a DNA N6-adenine methyltransferase from Helicobacter pylori
The structural basis underlying DNA N6-adenine methyltransferase substrate promiscuity was revealed and site-directed mutagenesis experiments identified residues D29 and E216 as crucial amino acids for cofactor binding and the methyl transfer activity of the enzyme. Expand
Specificity of restriction endonucleases and methylases--a review.
Large DNA fragments can be generated which is helpful in the construction of genomic libraries, and the design of novel sequence specificities are allowed. Expand
Single Turnover Kinetics of Methylation by T4 DNA-(N6-Adenine)-Methyltransferase
Interaction of T4 DNA-(N6-adenine)-methyltransferase was studied with a variety of synthetic oligonucleotide substrates containing the native recognition site GATC or its modified variants. The dataExpand
DNA (Cytosine-N 4-)- and -(Adenine-N 6-)-methyltransferases Have Different Kinetic Mechanisms but the Same Reaction Route
We studied the kinetics of methyl group transfer by the BamHI DNA-(cytosine-N 4-)-methyltransferase (MTase) from Bacillus amyloliquefaciens to a 20-mer oligodeoxynucleotide duplex containing theExpand
DNA methyltransferases: Mechanistic models derived from kinetic analysis
The sequence-specific transfer of methyl groups from donor S-adenosyl-L-methionine (AdoMet) to certain positions of DNA-adenine or -cytosine residues by DNA methyltransferases (MTases) is a majorExpand
Chemical modification of bovine pancreatic deoxyribonuclease with phenylglyoxal--the involvement of Arg-9 and Arg-41 in substrate binding.
It is concluded that Arg-27 and Arg-30 are essentially un-protected by DNA while Arg-9 andArg-41 are protected part of the time, which agrees with the proposed substrate binding site in the three-dimensional structure of DNase. Expand
DMI-1, a new DNA methyltransferase inhibitor produced by Streptomyces sp. strain No. 560.
DMI-1 is a novel inhibitor of methyltransferase isolated from microorganisms and is structurally different from sinefungin and A9145C which are structural analogs of S-adenosylmethionine (methyl donor). Expand
Specificity of restriction endonucleases and DNA modification methyltransferases a review (Edition 3).
The properties and sources of all known class-I, class-II and class-III restriction endonucleases (ENases) and DNA modification methyltransferases (MTases) are listed and newly subclassifiedExpand