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S-adenosyl-L-methionine + 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5
?
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S-adenosyl-L-methionine + 5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'
?
-
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
additional information
?
-
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
20-mer oligodeoxynucleotide duplex containing the palindromic recognition site GGATCC. The enzyme catalyzes methyl group transfer to the internal cytosine residue in the palindromic recognition site GGATCC. The enzyme transfers the methyl group to the exocyclic NH2-group without formation of a transient covalent bond
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'. The target base is the internal cytosine in the recognition sequence
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
20-mer duplex 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5' containing a palindromic recognition site GGATCC
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
M.BcnIA and M.BcnIB act on 5'-CC(C/G)GG-3' sites in double-stranded DNA. M.BcnIA can also, with a comparable efficiency, modify the specific targets in single-stranded DNA
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
substrate is pNH20 plasmid DNA. M2.MboII modifies the internal cytosine in the recognition sequence 39-CTTCT-59, yielding N4-methylcytosine, and moreover is able to methylate double- and single-stranded DNA, single-stranded DNA is preferred. Determination and analysis of the methylation pattern of M2.MboII, overview
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-
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
substrate is pNH20 plasmid DNA. M2.NcuI modifies the internal cytosine in the recognition sequence yielding N4-methylcytosine, and moreover is able to methylate double- and single-stranded DNA, single-stranded DNA is preferred. Determination of the methylation position, overview
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-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the enzyme generates N4-methylcytosine in duplex 5'-CAGCTG-3' DNA. PvuII methyltransferase is catalytically competent with one and with two bound molecules of S-adenosyl-L-methionine
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the enzyme catalyzes the transfer of the methyl group from S-adenosyl-L-methionine to the exocyclic aminoN4 nitrogen of the central cytosine in its recognition sequence 5'-CAGCTG-3'
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?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the enzyme modifies the second cytosine in CAGCTG sequences, also methylates adenine residues in CAGATG/CAGCTG substrates in which the target cytosine is replaced by adenine in one strand of the recognition sequence
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
substrate is methylated plasmid DNA. M.PspGI is a type IIP methyltransferase and enhances fluorescence of 2-aminopurine in DNA if it replaces the second C in the sequence
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage. SuaI is the only restriction-modification system detected in SUlfolobus acidocaldarius and the N4 methylation of the inner C in the recognition site is necessary and sufficient to protect against it
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage. SuaI is the only restriction-modification system detected in SUlfolobus acidocaldarius and the N4 methylation of the inner C in the recognition site is necessary and sufficient to protect against it
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
methylation of second cytosine of 5'-CCCGGG-3' recognition sequence
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
additional information
?
-
-
integrity of ATCC sequence is critical
-
-
?
additional information
?
-
-
the enzyme also displays promiscuous activity catalyzing methylation of adenine at the N6 position in DNA
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-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Klimasauskas, S.; Timinskas, A.; Menkevicius, S.; Butkiene, D.; Butkus, V.; Janulaitis, A.
Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases: similarity to adenine and cytosine-C5 DNA-methylases
Nucleic Acids Res.
17
9823-9832
1989
Citrobacter freundii, Kocuria varians, Citrobacter freundii RFL9, Kocuria varians RFL19
brenda
Roberts, R.J.; Macelis, D.
Restriction enzymes and their isoschizomers
Nucleic Acids Res.
20
2167-2180
1992
Bacteria
brenda
Malygin, E.G.; Zinoviev, V.V.; Evdokimov, A.A.; Lindstrom, W.M., Jr.; Reich, N.O.; Hattman, S.
DNA-(cytosine-N4)- and (adenine-N6)-methyltransferases have different kinetic mechanisms but the same reaction route: a comparison of M.BamHI and T4 Dam
J. Biol. Chem.
20
1-31
2003
Bacillus amyloliquefaciens
-
brenda
O'Gara, M.; Adams, G.M.; Gong, W.; Kobayashi, R.; Blumenthal, R.M.; Cheng, X.
Expression, purification, mass spectrometry, crystallization and multiwavelength anomalous diffraction of selenomethionyl PvuII DNA methyltransferase (cytosine-N4-specific)
Eur. J. Biochem.
247
1009-1018
1997
Proteus vulgaris
brenda
Zinoviev, V.V.; Evdokimov, A.A.; Malygin, E.G.
DNA-(N4-Cytosine)-methyltransferase from Bacillus amyloliquefaciens: mechanism of action derived from steady-state kinetics
Mol. Biol. (Mosk.)
37
116-124
2003
Bacillus amyloliquefaciens
-
brenda
Lindstrom, W.M., Jr.; Malygin, E.G.; Ovechkina, L.G.; Zinoviev, V.V.; Reich, N.O.
Functional analysis of BamHI DNA cytosine-N4 methyltransferase
J. Mol. Biol.
325
711-720
2003
Bacillus amyloliquefaciens
brenda
Adams, G.M.; Blumenthal, R.M.
The PvuII DNA (cytosine-N4)-methyltransferase comprises two trypsin-defined domains, each of which binds a molecule of S-adenosyl-L-methionine
Biochemistry
36
8284-8292
1997
Proteus vulgaris
brenda
Bujnicki, J.M.; Radlinska, M.
Molecular evolution of DNA-(cytosine-N4) methyltransferases: evidence for their polyphyletic origin
Nucleic Acids Res.
27
4501-4509
1999
Cenarchaeum symbiosum, Cenarchaeum symbiosum (O74074), Helicobacter pylori, Helicobacter pylori (Q9ZLF1), Lactobacillus phage phig1e, Methanocaldococcus jannaschii, Pseudomonas alcaligenes, Pyrococcus horikoshii, Salmonella enterica subsp. enterica serovar Typhi, Xanthomonas citri pv. malvacearum, Streptomyces fimbriatus (O52513), Streptomyces caespitosus (O52692), Saccharopolyspora sp. (O52711), Methanothermobacter wolfeii (O59647), Bacillus subtilis (O68556), Bacillus subtilis (Q45489), Gordonia rubripertincta (O85488), Pyrococcus sp. (O93645), Trichormus variabilis (P0A462), Proteus hauseri (P11409), Serratia marcescens (P14230), Citrobacter freundii (P14243), Citrobacter freundii (Q04845), Kocuria varians (P14244), Bacillus amyloliquefaciens (P18051), Bacillus amyloliquefaciens (P23941), Methanothermobacter thermautotrophicus (P29568), Xanthomonas campestris pv. cyanopsidis (P30774), Geobacillus stearothermophilus (P70986), Curtobacterium albidum (P71101), Halobacterium phage phiH (Q38204), Neisseria gonorrhoeae (Q9AKV2), Methanothermobacter thermautotrophicus Z-250 (P29568), Neisseria gonorrhoeae ME11 (Q9AKV2), Citrobacter freundii RFL9 (P14243), Bacillus amyloliquefaciens H (P23941), Citrobacter freundii 4111 (Q04845), Geobacillus stearothermophilus JN2091 (P70986), Kocuria varians RFL19 (P14244), Cenarchaeum symbiosum B (O74074), Cenarchaeum symbiosum A, Pseudomonas alcaligenes NCIB 986, Salmonella enterica subsp. enterica serovar Typhi CT18, Pyrococcus horikoshii OT-3
brenda
Gong, W.; O'Gara, M.; Blumenthal, R.M.; Cheng, X.
Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment
Nucleic Acids Res.
25
2702-2715
1997
Proteus vulgaris
brenda
Merkiene, E.; Vilkaitis, G.; Klimasauskas, S.
A pair of single-strand and double-strand DNA cytosine-N4 methyltransferases from Bacillus centrosporus
Biol. Chem.
379
569-571
1998
Brevibacillus centrosporus
brenda
Jeltsch, A.
The cytosine N4-methyltransferase M.PvuII also modifies adenine residues
Biol. Chem.
382
707-710
2001
Proteus vulgaris
brenda
Malygin, E.G.; Ovechkina, L.G.; Zinoviev, V.V.; Lindstrem, U.M.; Reich, N.O.
DNA-(N4-cytosine)-methyltransferase from Bacillus amyloliquefaciens: kinetic and substrate-binding properties
Mol. Biol. (Mosk.)
35
35-44
2001
Bacillus amyloliquefaciens
-
brenda
Zinoviev, V.V.; Yakishchik, S.I.; Evdokimov, A.A.; Malygin, E.G.; Hattman, S.
Symmetry elements in DNA structure important for recognition/methylation by DNA [amino]-methyltransferases
Nucleic Acids Res.
32
3930-3934
2004
Bacillus amyloliquefaciens
brenda
Yu, Y.J.; Yang, M.T.
A novel restriction-modification system from Xanthomonas campestris pv. vesicatoria encodes a m4C-methyltransferase and a nonfunctional restriction endonuclease
FEMS Microbiol. Lett.
272
83-90
2007
Xanthomonas campestris (Q3BWM2)
brenda
Carpenter, M.A.; Bhagwat, A.S.
DNA base flipping by both members of the PspGI restriction-modification system
Nucleic Acids Res.
36
5417-5425
2008
Pyrococcus sp. GI-H
brenda
Furmanek-Blaszk, B.; Boratynski, R.; Zolcinska, N.; Sektas, M.
M1.Mboll and M2.Mboll type IIS methyltransferases: different specificities, the same target
Microbiology
155
1111-1121
2009
Moraxella bovis, Moraxella cuniculi
brenda
Aranda, J.; Roca, M.; Lopez-Canut, V.; Tunon, I.
Theoretical study of the catalytic mechanism of DNA-(N4-cytosine)-methyltransferase from the bacterium Proteus vulgaris
J. Phys. Chem. B
114
8467-8473
2010
Proteus vulgaris
brenda
Clark, T.A.; Murray, I.A.; Morgan, R.D.; Kislyuk, A.O.; Spittle, K.E.; Boitano, M.; Fomenkov, A.; Roberts, R.J.; Korlach, J.
Characterization of DNA methyltransferase specificities using single-molecule, real-time DNA sequencing
Nucleic Acids Res.
40
e29
2012
Acetobacter aceti, Geobacillus stearothermophilus, uncultured bacterium, Cereibacter sphaeroides
brenda
Grogan, D.W.
Cytosine methylation by the SuaI restriction-modification system: implications for genetic fidelity in a hyperthermophilic archaeon
J. Bacteriol.
185
4657-4661
2003
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DG185
brenda
Aranda, J.; Roca, M.; Tunon, I.
Substrate promiscuity in DNA methyltransferase M.PvuII. A mechanistic insight
Org. Biomol. Chem.
10
5395-5400
2012
Proteus vulgaris
brenda
Furuta, Y.; Namba-Fukuyo, H.; Shibata, T.F.; Nishiyama, T.; Shigenobu, S.; Suzuki, Y.; Sugano, S.; Hasebe, M.; Kobayashi, I.
Methylome diversification through changes in DNA methyltransferase sequence specificity
PLoS Genet.
10
e1004272
2014
Helicobacter pylori
brenda
Chung, D.; Farkas, J.; Huddleston, J.R.; Olivar, E.; Westpheling, J.
Methylation by a unique alpha-class N4-cytosine methyltransferase is required for DNA transformation of Caldicellulosiruptor bescii DSM6725
PLoS ONE
7
e43844
2012
Caldicellulosiruptor bescii (B9MK94), Caldicellulosiruptor bescii, Caldicellulosiruptor bescii DSM 6725 (B9MK94)
brenda
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Cytosine N4-methylation via M.Ssp6803II is involved in the regulation of transcription, fine-tuning of DNA replication and DNA repair in the cyanobacterium Synechocystis sp. PCC 6803
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