Affinity modification of EcoRII dna methyltransferase by the dialdehyde-substituted DNA duplexes: Mapping the enzyme region that interacts with DNA

Nucleosides, Nucleotides and Nucleic Acids

Volumn 21, Issue 11-12, 2002, Pages 753-764

  Gritsenko, Oksana M ^a   Koudan, Elizaveta V ^a   Mikhailov, Sergey N ^b   Ermolinsky, Boris S ^b   Van Aerschot, Arthur ^c   Herdewijn, Pier ^c   Gromova, Elizaveta S ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^c REGA INSTITUTE FOR MEDICAL RESEARCH   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE DERIVATIVE; DNA METHYLTRANSFERASE; DOUBLE STRANDED DNA;

ARTICLE; BINDING AFFINITY; BINDING SITE; HYDROLYSIS; NUCLEOTIDE SEQUENCE; PROTEIN CROSS LINKING; PROTEIN DNA BINDING;

ALDEHYDES; BASE SEQUENCE; BINDING SITES; CROSS-LINKING REAGENTS; DNA; DNA METHYLATION; DNA-BINDING PROTEINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MOLECULAR SEQUENCE DATA; OLIGODEOXYRIBONUCLEOTIDES; SITE-SPECIFIC DNA METHYLTRANSFERASE (CYTOSINE-SPECIFIC);

EID: 0036917754     PISSN: 15257770     EISSN: None     Source Type: Journal    
DOI: 10.1081/NCN-120016478     Document Type: Article

References (18)

1. Klimašauskas, S.; Kumar, S.; Roberts, R.J.; Cheng, X. HhaI methyltransferase flips its target base out of the DNA helix. Cell 1994, 76, 357-369.
2. Reinisch, K.M.; Chen, L.; Verdine, G.L.; Lipscomb, W.N. The crystal structure of HaeIII methyltransferase convalently complexed to DNA: An extrahelical cytosine and rearranged base pairing. Cell 1995, 82, 143-153.
3. Dong, A.; Yoder, J.A.; Zhang, X.; Zhou, L.; Bestor, T.H.; Cheng, X. Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA. Nucleic Acids Res. 2001, 29, 439-448.
4. Kumar, S.; Cheng, X.; Klimašauskas, S.; Mi, S.; Posfai, J.; Roberts, R.; Wilson, G.G. The DNA (Cytosine-5) Methyltransferases. Nucleic Acids Res. 1994, 22, 1-10.
5. Som, S.; Bhagwat, A.S.; Friedman, S. Nucleotide sequence and expression of the gene encoding the EcoRII modification enzyme. Nucleic Acids Res. 1987, 15, 313-332.
6. Friedman, S.; Ansari, N. Binding of the EcoRII methyltransferase to 5-fluorocytosine-containing DNA. Isolation of a bound peptide. Nucleic Acids Res. 1992, 20, 3241-3248.
7. Wyszynski, M.W.; Gabbara, S.; Kubareva, E.A.; Romanova, E.A.; Oretskaya, T.S.; Gromova, E.S.; Shabarova, Z.A.; Bhagwat, A.S. The cysteine conserved among DNA cytosine methylases is required for methyl transfer, but not for specific DNA binding. Nucleic Acids Res. 1993, 21, 295-301.
8. Kossykh, V.G.; Schlagman, S.L.; Hattman, S. Function of Pro-185 in the ProCys of conserved Motif IV in the EcoRII [Cytosine-C5]-DNA methyltransferase. FEBS Lett. 1995, 370, 75-77.
9. Som, S.; Friedman, S. Identification of a Highly Conserved Domain in the EcoRII Methyltransferase which can be Photolabeled with S-Adenosyl-L-[Methyl-3H]Methionine. Evidence for UV-Induced Transmethylation of Cysteine 186. J. Biol. Chem. 1991, 266, 2937-2945.
10. Kiss, A.; Posfai, G.; Zsurka, G.; Rasko, T.; Venetianer, P. Role of DNA minor groove interactions in substrate recognition by the M·SinI and M·EcoRII DNA (Cytosine-5) methyltransferases. Nucleic Acids Res. 2001, 29, 3188-3194.
11. Brevnov, M.G.; Gritsenko, O.M.; Mikhailov, S.N.; Efimtseva, E.V.; Ermolinsky, B.S.; Van Aerschot, A.; Herdewijn, P.; Repyk, A.V.; Gromova, E.S. DNA duplexes with reactive dialdehyde groups as novel reagents for cross-linking to restriction-modification enzymes. Nucleic Acids Res. 1997, 25, 3302-3309.
12. Gritsenko, O.M.; Mikhailov, S.N.; Efimtseva, E.V.; Van Aerschot, A.; Herdewijn, P.; Gromova, E.S. Probing the MvaI methyltransferase region that interacts with DNA: Affinity labeling with the dialdehyde-containing DNA duplexes. Nucleosides, Nucleotides & Nucleic acids 2000, 19, 1805-1820.
13. Tunitskaya, V.L.; Rusakova, E.E.; Memelova, L.V.; Kochetkov, S.N.; Van Aerschot, A.; Herdewijn, P.; Efimtseva, E.V.; Ermolinsky, B.S.; Mikhailov, S.N. The mapping of T7 RNA polymerase active site with novel reagents - Oligonucleotides with Reactive dialdehyde groups. FEBS Lett. 1999, 442, 20-24.
14. Gritsenko, O.M.; Gromova, E.S. Dialdehyde-containing Nucleic acids and their components: Synthesis, properties and affinity modification of proteins. Russ. Chem. Rev. 1999, 68, 241-251.
15. Schroeder, S.G.; Samudzi, C.T. Structural Studies of EcoRII Methylase: Exploring Similarities among Methylases. Protein Eng. 1997, 10, 1385-1393.
16. Vilkaitis, G.; Dong, A.; Weinhold, E.; Cheng, X.; Klimašauskas, S. Functional roles of the conserved threonine 250 in the target recognition domain of HhaI DNA methyltransferase. J. Biol. Chem. 2000, 275, 38722-38730.
17. Babkina, O.V.; Evstafieva, A.G.; Chichkova, N.V.; Vartapetian, A.B.; Müller, S.; Baskunov, V.B.; Petrauskene, O.V.; Kochetkov, S.N.; Gromova, E.S. Recombinant components of the EcoRII restriction-modification system. Ability of restriction endonucleases to interact with DNA-RNA duplexes. Molecular Biology (Russ.) 2000, 34, 913-920.
18. Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 1970, 227, 680-685.