Functional roles of conserved amino acid residues in DNA methyltransferases investigated by site-directed mutagenesis of the EcoRV adenine-N6-methyltransferase (Q47892200)

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scientific article published in July 1998

Language	Label	Description	Also known as
English	Functional roles of conserved amino acid residues in DNA methyltransferases investigated by site-directed mutagenesis of the EcoRV adenine-N6-methyltransferase	scientific article published in July 1998

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

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

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

4

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

author name string

Roth M

1

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

Helm-Kruse S

2

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

Friedrich T

3

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

language of work or name

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publication date

1 July 1998

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

273

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

28

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

17333-17342

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

describes a project that uses

site-directed mutagenesis

1 reference

based on heuristic

inferred from title

Eukaryotic DNA methyltransferases--structure and function

1 reference

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

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

1 reference

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DNA methylation and genomic imprinting

1 reference

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21 January 2018

Structure and function of DNA methyltransferases.

1 reference

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21 January 2018

Chemistry and biology of DNA methyltransferases

1 reference

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21 January 2018

The DNA (cytosine-5) methyltransferases

1 reference

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21 January 2018

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

1 reference

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21 January 2018

HhaI methyltransferase flips its target base out of the DNA helix

1 reference

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21 January 2018

Enzymatic C5-cytosine methylation of DNA: mechanistic implications of new crystal structures for HhaL methyltransferase-DNA-AdoHcy complexes

1 reference

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21 January 2018

A structural basis for the preferential binding of hemimethylated DNA by HhaI DNA methyltransferase

1 reference

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21 January 2018

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

1 reference

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21 January 2018

The GATATC-modification enzyme EcoRV is closely related to the GATC-recognizing methyltransferases DpnII and dam from E. coli and phage T4.

1 reference

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21 January 2018

Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases: similarity to adenine and cytosine-C5 DNA-methylases

1 reference

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21 January 2018

Finding sequence motifs in groups of functionally related proteins

1 reference

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21 January 2018

Amino acid sequence arrangements of DNA-methyltransferases

1 reference

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21 January 2018

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

1 reference

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21 January 2018

The role of the preserved sequences of Dam methylase

1 reference

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21 January 2018

Functional analysis of conserved motifs in EcoP15I DNA methyltransferase

1 reference

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21 January 2018

Substrate DNA and cofactor regulate the activities of a multi-functional restriction-modification enzyme, BcgI.

1 reference

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21 January 2018

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

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Universal catalytic domain structure of AdoMet-dependent methyltransferases.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Targeted base stacking disruption by the EcoRI DNA methyltransferase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

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

1 reference

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21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

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

1 reference

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21 January 2018

Incorporation of a complete set of deoxyadenosine and thymidine analogues suitable for the study of protein nucleic acid interactions into oligodeoxynucleotides. Application to the EcoRV restriction endonuclease and modification methylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Sequence-specific binding of DNA by the EcoRV restriction and modification enzymes with nucleic acid and cofactor analogues

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Probing the protein-DNA interface of the EcoRV modification methyltransferase bound to its recognition sequence, GATATC.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction

1 reference

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21 January 2018

Functional mapping of the EcoRV DNA methyltransferase by random mutagenesis and screening for catalytically inactive mutants

1 reference

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21 January 2018

Crystal structure of catechol O-methyltransferase

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21 January 2018

The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends

1 reference

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21 January 2018

Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine

1 reference

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21 January 2018

Sequence-specific DNA binding by the MspI DNA methyltransferase

1 reference

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21 January 2018

Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI

1 reference

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21 January 2018

Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with known structures of methyltransferases and isolation of catalytically inactive single mutants

1 reference

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21 January 2018

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

1 reference

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21 January 2018

The EcoRV modification methylase causes considerable bending of DNA upon binding to its recognition sequence GATATC

1 reference

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21 January 2018

Identifiers

10.1074/JBC.273.28.17333

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9651316

ResearchGate publication ID

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