Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-6-26
pubmed:abstractText
Previous comparison of the amino acid sequences of the GATC-methylating Escherichia coli Dam methyltransferase (MTase) with those of other adenine MTases (M.EcoRV, M.DpnII and T4Dam) localized four conserved regions. Regions III and IV have similarities with many other MTases. The sequence DPPY (or NPPY) is always present in region IV. It was suggested to be the AdoMet binding site. Publication of the nucleotide and amino acid sequences of M.CviBIII, M.DpnA and MutH give further credence to this assignment: M.DpnA, which also methylates GATC, has strong similarities with regions III and IV; M.CviBIII, a cytosine methylase, has a characteristic NPPY sequence in region IV, and only limited resemblance in region III; MutH, the GATC-specific endonuclease in DNA mismatch repair, has significant similarities uniquely in region III. The presently available evidence suggests that region III is the GAT(C) binding site and region IV is the AdoMet binding site. This hypothesis is strengthened by recent genetic findings.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/DNA Modification Methylases, http://linkedlifedata.com/resource/pubmed/chemical/DNA Repair Enzymes, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dam methyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/S-Adenosylmethionine, http://linkedlifedata.com/resource/pubmed/chemical/Site-Specific..., http://linkedlifedata.com/resource/pubmed/chemical/dam protein, E coli
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
211-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:3074010-Amino Acid Sequence, pubmed-meshheading:3074010-Bacterial Proteins, pubmed-meshheading:3074010-Binding Sites, pubmed-meshheading:3074010-DNA, Bacterial, pubmed-meshheading:3074010-DNA Modification Methylases, pubmed-meshheading:3074010-DNA Repair, pubmed-meshheading:3074010-DNA Repair Enzymes, pubmed-meshheading:3074010-DNA-Binding Proteins, pubmed-meshheading:3074010-Endodeoxyribonucleases, pubmed-meshheading:3074010-Escherichia coli, pubmed-meshheading:3074010-Escherichia coli Proteins, pubmed-meshheading:3074010-Methyltransferases, pubmed-meshheading:3074010-Molecular Sequence Data, pubmed-meshheading:3074010-Protein Binding, pubmed-meshheading:3074010-Protein Conformation, pubmed-meshheading:3074010-S-Adenosylmethionine, pubmed-meshheading:3074010-Sequence Homology, Nucleic Acid, pubmed-meshheading:3074010-Site-Specific DNA-Methyltransferase (Adenine-Specific)
pubmed:year
1988
pubmed:articleTitle
The DNA and S-adenosylmethionine-binding regions of EcoDam and related methyltransferases.
pubmed:affiliation
Département de Biologie, Centre d'Etudes Nucléaires de Saclay, Gif-sur-Yvette, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't