A symmetrical model for the domain structure of type I DNA methyltransferases.
about
Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle)Nucleoside triphosphate-dependent restriction enzymesPurification and characterisation of a novel DNA methyltransferase, M.AhdIThe structure of M.EcoKI Type I DNA methyltransferase with a DNA mimic antirestriction proteinStructure of HsdS Subunit from Thermoanaerobacter tengcongensis Sheds Lights on Mechanism of Dynamic Opening and Closing of Type I MethyltransferaseProtein footprinting approach to mapping DNA binding sites of two archaeal homing enzymes: evidence for a two-domain protein structure.Families of restriction enzymes: an analysis prompted by molecular and genetic data for type ID restriction and modification systems.Tracking EcoKI and DNA fifty years on: a golden story full of surprises.Crystal structure of DNA sequence specificity subunit of a type I restriction-modification enzyme and its functional implications.Structure and operation of the DNA-translocating type I DNA restriction enzymes.A prediction of the amino acids and structures involved in DNA recognition by type I DNA restriction and modification enzymes.S-adenosyl methionine alters the DNA contacts of the EcoKI methyltransferase.Tyrosine 27 of the specificity polypeptide of EcoKI can be UV crosslinked to a bromodeoxyuridine-substituted DNA target sequence.Deletion of one nucleotide within the homonucleotide tract present in the hsdS gene alters the DNA sequence specificity of type I restriction-modification system NgoAVEcoR124I: from plasmid-encoded restriction-modification system to nanodevice.Diversity of DNA methyltransferases that recognize asymmetric target sequences.Interaction of the type I methyltransferase M.EcoR124I with modified DNA substrates: sequence discrimination and base flipping.Protein-protein and protein-DNA interactions in the type I restriction endonuclease R.EcoR124I.A type IC restriction-modification system in Lactococcus lactis.Interaction of the ocr gene 0.3 protein of bacteriophage T7 with EcoKI restriction/modification enzyme.High resolution footprinting of a type I methyltransferase reveals a large structural distortion within the DNA recognition site.DNA binding and subunit interactions in the type I methyltransferase M.EcoR124I.The specificity of sty SKI, a type I restriction enzyme, implies a structure with rotational symmetry.Structural and functional analysis of the engineered type I DNA methyltransferase EcoR124I(NT)DNA-binding induces a major structural transition in a type I methyltransferase.Shape and subunit organisation of the DNA methyltransferase M.AhdI by small-angle neutron scattering.Genomic structure of the human DNA methyltransferase gene.Repercussions of DNA tracking by the type IC restriction endonuclease EcoR124I on linear, circular and catenated substrates.Organization of the BcgI restriction-modification protein for the cleavage of eight phosphodiester bonds in DNA.Organization of the BcgI restriction-modification protein for the transfer of one methyl group to DNA.Removal of a frameshift between the hsdM and hsdS genes of the EcoKI Type IA DNA restriction and modification system produces a new type of system and links the different families of Type I systems.Structural model for the multisubunit Type IC restriction-modification DNA methyltransferase M.EcoR124I in complex with DNA.Analysis of type I restriction modification systems in the Neisseriaceae: genetic organization and properties of the gene products.Functional analysis of MmeI from methanol utilizer Methylophilus methylotrophus, a subtype IIC restriction-modification enzyme related to type I enzymes.Genome-wide analysis of restriction-modification system in unicellular and filamentous cyanobacteria.Novel type I restriction specificities through domain shuffling of HsdS subunits in Lactococcus lactis.Expression and characterisation of the N-terminal fragment of the HsdS subunit of M.EcoR124I.Combinational variation of restriction modification specificities in Lactococcus lactis.Structures of the type I DNA restriction enzymes.A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes
P2860
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P2860
A symmetrical model for the domain structure of type I DNA methyltransferases.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
A symmetrical model for the domain structure of type I DNA methyltransferases.
@en
type
label
A symmetrical model for the domain structure of type I DNA methyltransferases.
@en
prefLabel
A symmetrical model for the domain structure of type I DNA methyltransferases.
@en
P356
P1476
A symmetrical model for the domain structure of type I DNA methyltransferases.
@en
P2093
P356
10.1006/JMBI.1994.1624
P407
P577
1994-10-01T00:00:00Z