A mutational analysis of the two motifs common to adenine methyltransferases.
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Induction of sporulation in Saccharomyces cerevisiae leads to the formation of N6-methyladenosine in mRNA: a potential mechanism for the activity of the IME4 gene.Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle)Nucleoside triphosphate-dependent restriction enzymesRegulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymesDNA bending by M.EcoKI methyltransferase is coupled to nucleotide flipping.Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases.The structure of M.EcoKI Type I DNA methyltransferase with a DNA mimic antirestriction proteinStructural Basis for Binding of RNA and Cofactor by a KsgA MethyltransferaseThe human tRNA(m(2)(2)G(26))dimethyltransferase: functional expression and characterization of a cloned hTRM1 geneUnusual 2-aminopurine fluorescence from a complex of DNA and the EcoKI methyltransferase.KpnBI is the prototype of a new family (IE) of bacterial type I restriction-modification system.Tracking EcoKI and DNA fifty years on: a golden story full of surprises.Yeast 18S rRNA dimethylase Dim1p: a quality control mechanism in ribosome synthesis?DNA translocation blockage, a general mechanism of cleavage site selection by type I restriction enzymes.Complete nucleotide sequence of the 27-kilobase virulence related locus (vrl) of Dichelobacter nodosus: evidence for extrachromosomal origin.The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors.S-adenosyl methionine alters the DNA contacts of the EcoKI methyltransferase.A mutant HpaII methyltransferase functions as a mutator enzyme.DNA methylation impacts gene expression and ensures hypoxic survival of Mycobacterium tuberculosis.Mutations within the catalytic motif of DNA adenine methyltransferase (Dam) of Aeromonas hydrophila cause the virulence of the Dam-overproducing strain to revert to that of the wild-type phenotype.Structure, function and mechanism of exocyclic DNA methyltransferases.Biochemical and structural characterization of a DNA N6-adenine methyltransferase from Helicobacter pyloriDual function of the tRNA(m(5)U54)methyltransferase in tRNA maturation.NmeSI restriction-modification system identified by representational difference analysis of a hypervirulent Neisseria meningitidis strain.A type IC restriction-modification system in Lactococcus lactis.The specificity of sty SKI, a type I restriction enzyme, implies a structure with rotational symmetry.Substrate DNA and cofactor regulate the activities of a multi-functional restriction-modification enzyme, BcgI.Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activitiesA motif conserved among the type I restriction-modification enzymes and antirestriction proteins: a possible basis for mechanism of action of plasmid-encoded antirestriction functions.Restriction by EcoKI is enhanced by co-operative interactions between target sequences and is dependent on DEAD box motifs.Probing the S-adenosylmethionine-binding site of rat guanidinoacetate methyltransferase. Effect of site-directed mutagenesis of residues that are conserved across mammalian non-nucleic acid methyltransferases.
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A mutational analysis of the two motifs common to adenine methyltransferases.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 1994
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
A mutational analysis of the two motifs common to adenine methyltransferases.
@en
A mutational analysis of the two motifs common to adenine methyltransferases.
@nl
type
label
A mutational analysis of the two motifs common to adenine methyltransferases.
@en
A mutational analysis of the two motifs common to adenine methyltransferases.
@nl
prefLabel
A mutational analysis of the two motifs common to adenine methyltransferases.
@en
A mutational analysis of the two motifs common to adenine methyltransferases.
@nl
P2093
P2860
P1433
P1476
A mutational analysis of the two motifs common to adenine methyltransferases
@en
P2093
P2860
P304
P356
10.1002/J.1460-2075.1994.TB06701.X
P407
P577
1994-08-01T00:00:00Z