Literature DB >> 2744483

M.FokI methylates adenine in both strands of its asymmetric recognition sequence.

D Landry1, M C Looney, G R Feehery, B E Slatko, W E Jack, I Schildkraut, G G Wilson.   

Abstract

M.FokI, a type-IIS modification enzyme from Flavobacterium okeanokoites, was purified, and its activity was characterized in vitro. The enzyme was found to be a DNA-adenine methyltransferase and to methylate both strands of the asymmetric FokI recognition sequence: (formula; see text) M.FokI does not methylate single-stranded DNA, nor does it methylate double-stranded DNA at sequences other than FokI sites.

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Year:  1989        PMID： 2744483     DOI： 10.1016/0378-1119(89)90353-3

Source DB:  PubMed          Journal:  Gene        ISSN： 0378-1119            Impact factor:   3.688


  15 in total

1.  The FokI methyltransferase from Flavobacterium okeanokoites. Purification and characterization of the enzyme and its truncated derivatives.

Authors:  T Kaczorowski; M Sektas; P Skowron; A J Podhajska
Journal:  Mol Biotechnol       Date:  1999-11       Impact factor: 2.695

2.  Alw26I, Eco31I and Esp3I--type IIs methyltransferases modifying cytosine and adenine in complementary strands of the target DNA.

Authors:  J Bitinaite; Z Maneliene; S Menkevicius; S Klimasauskas; V Butkus; A Janulaitis
Journal:  Nucleic Acids Res       Date:  1992-10-11       Impact factor: 16.971

3.  Effect of site-specific methylation on DNA modification methyltransferases and restriction endonucleases.

Authors:  M McClelland; M Nelson
Journal:  Nucleic Acids Res       Date:  1992-05-11       Impact factor: 16.971

Review 4.  Organization of restriction-modification systems.

Authors:  G G Wilson
Journal:  Nucleic Acids Res       Date:  1991-05-25       Impact factor: 16.971

5.  Site-specific methylation: effect on DNA modification methyltransferases and restriction endonucleases.

Authors:  M Nelson; M McClelland
Journal:  Nucleic Acids Res       Date:  1991-04-25       Impact factor: 16.971

6.  Characterization of the cloned BamHI restriction modification system: its nucleotide sequence, properties of the methylase, and expression in heterologous hosts.

Authors:  J E Brooks; P D Nathan; D Landry; L A Sznyter; P Waite-Rees; C L Ives; L S Moran; B E Slatko; J S Benner
Journal:  Nucleic Acids Res       Date:  1991-02-25       Impact factor: 16.971

7.  In vivo genetic exchange of a functional domain from a type II A methylase between lactococcal plasmid pTR2030 and a virulent bacteriophage.

Authors:  C Hill; L A Miller; T R Klaenhammer
Journal:  J Bacteriol       Date:  1991-07       Impact factor: 3.490

8.  Restriction enzymes and their isoschizomers.

Authors:  R J Roberts
Journal:  Nucleic Acids Res       Date:  1990-04-25       Impact factor: 16.971

9.  Determination of methylation specificity of DsaV methyltransferase by a simple biochemical method.

Authors:  J Gopal; A S Bhagwat
Journal:  Nucleic Acids Res       Date:  1995-01-11       Impact factor: 16.971

10.  BaeI, another unusual BcgI-like restriction endonuclease.

Authors:  L E Sears; B Zhou; J M Aliotta; R D Morgan; H Kong
Journal:  Nucleic Acids Res       Date:  1996-09-15       Impact factor: 16.971
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