Primary structure and strand specificity of BstF5I-1 DNA methyltransferase which recognizes 5'-GGATG-3'.

scientific article published in March 1997

Primary structure and strand specificity of BstF5I-1 DNA methyltransferase which recognizes 5'-GGATG-3'. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/S0378-1119(96)00752-4
P698PubMed publication ID9099883

P50authorAlla V. ShevchenkoQ73215587
P2093author name stringM A Abdurashitov
N A Netesova
S Kh Degtyarev
P2860cites workSequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferasesQ34299649
An improved technique for the efficient construction of gene libraries by partial filling-in of cohesive endsQ36425232
Cloning and sequence analysis of the StsI restriction-modification gene: presence of homology to FokI restriction-modification enzymesQ40533662
BstF5I, an unusual isoschizomer of FokI.Q43023893
Nucleotide sequence of the FokI restriction-modification system: separate strand-specificity domains in the methyltransferaseQ48289621
The pMTL nic- cloning vectors. I. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencingQ48317540
P433issue2
P407language of work or nameEnglishQ1860
P304page(s)217-219
P577publication date1997-03-01
P1433published inGeneQ5531065
P1476titlePrimary structure and strand specificity of BstF5I-1 DNA methyltransferase which recognizes 5'-GGATG-3'
P478volume187

Reverse relations

cites work (P2860)
Q39488949Characterization of the type IV restriction modification system BspLU11III from Bacillus sp. LU11.
Q37698622Diversity of DNA methyltransferases that recognize asymmetric target sequences
Q35079744Methylation by a mutant T2 DNA [N(6)-adenine] methyltransferase expands the usage of RecA-assisted endonuclease (RARE) cleavage
Q33984795Molecular characterization of a phage-encoded resistance system in Lactococcus lactis
Q43027269The archaeal halophilic virus-encoded Dam-like methyltransferase M. phiCh1-I methylates adenine residues and complements dam mutants in the low salt environment of Escherichia coli.

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