Zobrazeno 1 - 10
of 17
pro vyhledávání: '"N O, Reich"'
Autor:
Patricia J. Greene, Paul W. Hager, Herbert W. Boyer, T G Coche, N O Reich, Joseph P. Day, J M Rosenberg
Publikováno v:
Journal of Biological Chemistry. 265:21520-21526
The x-ray structure of the EcoRI endonuclease-DNA complex (3) suggests that hydrogen bonds between amino acids, glutamic acid 144, arginine 145, and arginine 200, and major groove base moieties are the molecular determinants of specificity. We have i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c90e8bcd98f640a8c99df3368f877664
https://doi.org/10.1016/s0021-9258(18)45770-5
https://doi.org/10.1016/s0021-9258(18)45770-5
Publikováno v:
Molekuliarnaia biologiia. 35(1)
Interaction of DNA-(N4-cytosine)-methyltransferase from the Bacillus amyloliquefaciens (BamHI MTase, 49 kDa) with a 20-mer oligonucleotide duplex containing the palindrome recognition site GGATCC was studied by methods of steady-state and presteady-s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ceab2eb52546d2b928b27d646bf45687
https://pubmed.ncbi.nlm.nih.gov/11234382
https://pubmed.ncbi.nlm.nih.gov/11234382
Publikováno v:
Nature structural biology. 6(3)
Specific recognition by EcoRV endonuclease of its cognate, sharply bent GATATC site at the center TA step occurs solely via hydrophobic interaction with thymine methyl groups. Mechanistic kinetic analyses of base analog-substituted DNAs at this posit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dfd87f3ce8f4a2b44583f9b001b89a6d
https://pubmed.ncbi.nlm.nih.gov/10074946
https://pubmed.ncbi.nlm.nih.gov/10074946
Autor:
N O, Reich, N, Mashhoon
Publikováno v:
The Journal of biological chemistry. 268(13)
We present the first presteady state kinetic analysis of an S-adenosylmethionine-dependent enzyme. The target enzyme is the bacterial EcoRI DNA methyl-transferase, which transfers the methyl group to the second adenine in the DNA sequence GAATTC. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6fea7b3e6de448ec44479e0850342e81
https://pubmed.ncbi.nlm.nih.gov/8486619
https://pubmed.ncbi.nlm.nih.gov/8486619
Publikováno v:
The Journal of biological chemistry. 267(26)
EcoRI DNA methyltransferase contains tryptophans at positions 183 and 225. Tryptophan 225 is adjacent to residues previously implicated in S-adenosylmethionine (AdoMet) binding and to cysteine 223, previously shown to be the site of N-ethyl maleimide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::90060a812de258442b96c6025e44c1f6
https://pubmed.ncbi.nlm.nih.gov/1526989
https://pubmed.ncbi.nlm.nih.gov/1526989
Publikováno v:
The Journal of biological chemistry. 267(22)
The sequence selectivity of enzyme-DNA interactions was analyzed by comparing discrimination between synthetic oligonucleotides containing the canonical site GAATTC and altered DNA sequences with the EcoRI DNA methyltransferase. The specificities (kc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4950350a72bb5cbc584522db26ff9ea6
https://pubmed.ncbi.nlm.nih.gov/1639813
https://pubmed.ncbi.nlm.nih.gov/1639813
Publikováno v:
The Journal of biological chemistry. 265(35)
The x-ray structure of the EcoRI endonuclease-DNA complex (3) suggests that hydrogen bonds between amino acids, glutamic acid 144, arginine 145, and arginine 200, and major groove base moieties are the molecular determinants of specificity. We have i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::db4f3033e1187684ff58c28451138995
https://pubmed.ncbi.nlm.nih.gov/2254311
https://pubmed.ncbi.nlm.nih.gov/2254311
Publikováno v:
The Journal of biological chemistry. 265(29)
EcoRI DNA methyltransferase (MTase) is rapidly inactivated by N-ethylmaleimide with concomitant incorporation of 2 mol of N-ethyl[2-3H]maleimide/mol of functional monomer. Preincubation of the enzyme with either S-adenosylmethionine or DNA reduces th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ad8747b7861cfa2aa8892ea866c49aa1
https://pubmed.ncbi.nlm.nih.gov/2170393
https://pubmed.ncbi.nlm.nih.gov/2170393
Autor:
N O, Reich, N, Mashhoon
Publikováno v:
The Journal of biological chemistry. 265(15)
Four analogs of the natural cofactor S-adenosylmethionine (AdoMet) were tested for their ability to bind and inhibit the prokaryotic enzyme, EcoRI adenine DNA methylase. The EcoRI methylase transfers the methyl group from AdoMet to the second adenine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::50501bf79091eb70515934365fa2ac05
https://pubmed.ncbi.nlm.nih.gov/2341414
https://pubmed.ncbi.nlm.nih.gov/2341414
Autor:
N O, Reich, E A, Everett
Publikováno v:
The Journal of biological chemistry. 265(15)
The Mr 38,050 monomeric EcoRI DNA methylase is part of a bacterial restriction-modification system. The methylase transfers the methyl group from S-adenosylmethionine (AdoMet) to the second adenine in the double-stranded DNA sequence 5'-GAATTC-3'. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b0876a9b2f6ec5c3905ab967d3416da1
https://pubmed.ncbi.nlm.nih.gov/2341412
https://pubmed.ncbi.nlm.nih.gov/2341412