On the Substrate Specificity of DNA Methyltransferases (Q57267693)

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9 December 2019

title

On the substrate specificity of DNA methyltransferases. adenine-N6 DNA methyltransferases also modify cytosine residues at position N4 (English)

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9 December 2019

1

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9 December 2019

author name string

F Christ

series ordinal

2

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9 December 2019

M Fatemi

series ordinal

3

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9 December 2019

M Roth

series ordinal

4

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9 December 2019

language of work or name

English

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publication date

1 July 1999

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Journal of Biological Chemistry

9 December 2019

published in

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9 December 2019

volume

274

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9 December 2019

issue

28

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9 December 2019

page(s)

19538-19544

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DNA methylation and genomic imprinting

9 December 2019

cites work

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Gametic imprinting in mammals

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X-chromosome inactivation: molecular mechanisms and genetic consequences

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Effects of DNA methylation on DNA-binding proteins and gene expression.

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Alterations in DNA methylation may play a variety of roles in carcinogenesis

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The role of DNA methylation in cancer genetic and epigenetics

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Altered DNA methylation and genome instability: a new pathway to cancer?

21 January 2018

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Targeted mutation of the DNA methyltransferase gene results in embryonic lethality

21 January 2018

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Strand-specific Mismatch Repair in Mammalian Cells

21 January 2018

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DNA modification by methyltransferases

21 January 2018

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Structure and Function of DNA Methyltransferases

21 January 2018

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Amino acid sequence arrangements of DNA-methyltransferases

21 January 2018

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The DNA (cytosine-5) methyltransferases

21 January 2018

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Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes

21 January 2018

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Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine

21 January 2018

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The crystal structure of Haelll methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing

21 January 2018

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Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment

21 January 2018

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Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine

21 January 2018

1 reference

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Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine

21 January 2018

1 reference

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HhaI methyltransferase flips its target base out of the DNA helix

21 January 2018

1 reference

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A model for DNA binding and enzyme action derived from crystallographic studies of the TaqI N6-adenine-methyltransferase

21 January 2018

1 reference

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Universal catalytic domain structure of AdoMet-dependent methyltransferases.

21 January 2018

1 reference

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Targeted base stacking disruption by the EcoRI DNA methyltransferase

21 January 2018

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Direct Real Time Observation of Base Flipping by theEcoRI DNA Methyltransferase

21 January 2018

1 reference

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2-Aminopurine as a fluorescent probe for DNA base flipping by methyltransferases

21 January 2018

1 reference

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Chemical display of thymine residues flipped out by DNA methyltransferases

21 January 2018

1 reference

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DNA distortion and base flipping by the EcoRV DNA methyltransferase. A study using interference at dA and T bases and modified deoxynucleosides

21 January 2018

1 reference

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Kinetics of methylation and binding of DNA by the EcoRV adenine-N6 methyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.274.28.19538

Mutational analysis of target base flipping by the EcoRV adenine-N6 DNA methyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.274.28.19538

M.HhaI binds tightly to substrates containing mismatches at the target base

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.274.28.19538

HhaI and HpaII DNA methyltransferases bind DNA mismatches, methylate uracil and block DNA repair

21 January 2018

1 reference

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The Flavobacterium okeanokoites adenine-N6-specific DNA-methyltransferase M.FokI is a tandem enzyme of two independent domains with very different kinetic properties.

21 January 2018

1 reference

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The cloning, purification and characterization of the Eco RV modification methylase

21 January 2018

1 reference

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Nucleotide sequence of the FokI restriction-modification system: separate strand-specificity domains in the methyltransferase

21 January 2018

1 reference

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New restriction endonucleases from Flavobacterium okeanokoites (FokI) and Micrococcus luteus (MluI).

21 January 2018

1 reference

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Sequence-Specific Binding of DNA by the EcoRV Restriction and Modification Enzymes with Nucleic Acid and Cofactor Analogs

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.274.28.19538

Functional roles of conserved amino acid residues in DNA methyltransferases investigated by site-directed mutagenesis of the EcoRV adenine-N6-methyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.274.28.19538

Investigation of ionizable residues critical for sequence-specific enzymatic DNA modification: protein modification and steady-state and pre-steady-state kinetic pH analyses of EcoRI DNA methyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.274.28.19538

21 January 2018

Identifiers

DOI

10.1074/JBC.274.28.19538

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10391886 AND SRC:MED&resulttype=core&format=json

9 December 2019

1 reference