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. 1997 May 15;25(10):2025–2029. doi: 10.1093/nar/25.10.2025

Angle and locus of the bend induced by the msp I DNA methyltransferase in a sequence-specific complex with DNA.

A K Dubey 1, S K Bhattacharya 1
PMCID: PMC146686  PMID: 9115372

Abstract

Bending of DNA induced by M.Msp I, one of the m5C-DNA methyltransferases, has been investigated using circular permutation analysis. The M.Msp I MTase induced sharp bends in DNA containing its recognition sequence 5'-CCGG-3'which was estimated to be 142+/-4 degrees and 132+/-4 degrees for circularly permuted DNA fragments of 127 and 1459 bp respectively. The bend centre was found to be asymmetric with respect to the CCGG sequence and appeared to exclude the 'target cytosine'. An estimate of approximately 15 kcal/mol was obtained for the free energy associated with M.Msp I-induced DNA bending.

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Selected References

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  1. Aiken C. R., Fisher E. W., Gumport R. I. The specific binding, bending, and unwinding of DNA by RsrI endonuclease, an isoschizomer of EcoRI endonuclease. J Biol Chem. 1991 Oct 5;266(28):19063–19069. [PubMed] [Google Scholar]
  2. Ansari A. Z., Bradner J. E., O'Halloran T. V. DNA-bend modulation in a repressor-to-activator switching mechanism. Nature. 1995 Mar 23;374(6520):371–375. doi: 10.1038/374370a0. [DOI] [PubMed] [Google Scholar]
  3. Chen L., MacMillan A. M., Chang W., Ezaz-Nikpay K., Lane W. S., Verdine G. L. Direct identification of the active-site nucleophile in a DNA (cytosine-5)-methyltransferase. Biochemistry. 1991 Nov 19;30(46):11018–11025. doi: 10.1021/bi00110a002. [DOI] [PubMed] [Google Scholar]
  4. Cheng X., Kumar S., Posfai J., Pflugrath J. W., Roberts R. J. Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine. Cell. 1993 Jul 30;74(2):299–307. doi: 10.1016/0092-8674(93)90421-l. [DOI] [PubMed] [Google Scholar]
  5. Chow C. S., Whitehead J. P., Lippard S. J. HMG domain proteins induce sharp bends in cisplatin-modified DNA. Biochemistry. 1994 Dec 20;33(50):15124–15130. doi: 10.1021/bi00254a023. [DOI] [PubMed] [Google Scholar]
  6. Depew D. E., Wang J. C. Conformational fluctuations of DNA helix. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4275–4279. doi: 10.1073/pnas.72.11.4275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Diekmann S. Temperature and salt dependence of the gel migration anomaly of curved DNA fragments. Nucleic Acids Res. 1987 Jan 12;15(1):247–265. doi: 10.1093/nar/15.1.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Diekmann S., Wang J. C. On the sequence determinants and flexibility of the kinetoplast DNA fragment with abnormal gel electrophoretic mobilities. J Mol Biol. 1985 Nov 5;186(1):1–11. doi: 10.1016/0022-2836(85)90251-7. [DOI] [PubMed] [Google Scholar]
  9. Dubey A. K., Mollet B., Roberts R. J. Purification and characterization of the MspI DNA methyltransferase cloned and overexpressed in E. coli. Nucleic Acids Res. 1992 Apr 11;20(7):1579–1585. doi: 10.1093/nar/20.7.1579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Dubey A. K., Roberts R. J. Sequence-specific DNA binding by the MspI DNA methyltransferase. Nucleic Acids Res. 1992 Jun 25;20(12):3167–3173. doi: 10.1093/nar/20.12.3167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Echols H. Multiple DNA-protein interactions governing high-precision DNA transactions. Science. 1986 Sep 5;233(4768):1050–1056. doi: 10.1126/science.2943018. [DOI] [PubMed] [Google Scholar]
  12. Garcia R. A., Bustamante C. J., Reich N. O. Sequence-specific recognition of cytosine C5 and adenine N6 DNA methyltransferases requires different deformations of DNA. Proc Natl Acad Sci U S A. 1996 Jul 23;93(15):7618–7622. doi: 10.1073/pnas.93.15.7618. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kim R., Modrich P., Kim S. H. 'Interactive' recognition in EcoRI restriction enzyme-DNA complex. Nucleic Acids Res. 1984 Oct 11;12(19):7285–7292. doi: 10.1093/nar/12.19.7285. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Klimasauskas S., Kumar S., Roberts R. J., Cheng X. HhaI methyltransferase flips its target base out of the DNA helix. Cell. 1994 Jan 28;76(2):357–369. doi: 10.1016/0092-8674(94)90342-5. [DOI] [PubMed] [Google Scholar]
  15. Koo H. S., Wu H. M., Crothers D. M. DNA bending at adenine . thymine tracts. Nature. 1986 Apr 10;320(6062):501–506. doi: 10.1038/320501a0. [DOI] [PubMed] [Google Scholar]
  16. Kumar S., Cheng X., Klimasauskas S., Mi S., Posfai J., Roberts R. J., Wilson G. G. The DNA (cytosine-5) methyltransferases. Nucleic Acids Res. 1994 Jan 11;22(1):1–10. doi: 10.1093/nar/22.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Lin P. M., Lee C. H., Roberts R. J. Cloning and characterization of the genes encoding the MspI restriction modification system. Nucleic Acids Res. 1989 Apr 25;17(8):3001–3011. doi: 10.1093/nar/17.8.3001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Liu-Johnson H. N., Gartenberg M. R., Crothers D. M. The DNA binding domain and bending angle of E. coli CAP protein. Cell. 1986 Dec 26;47(6):995–1005. doi: 10.1016/0092-8674(86)90814-7. [DOI] [PubMed] [Google Scholar]
  19. Lumpkin O. J., Déjardin P., Zimm B. H. Theory of gel electrophoresis of DNA. Biopolymers. 1985 Aug;24(8):1573–1593. doi: 10.1002/bip.360240812. [DOI] [PubMed] [Google Scholar]
  20. Matsuo K., Silke J., Gramatikoff K., Schaffner W. The CpG-specific methylase SssI has topoisomerase activity in the presence of Mg2+. Nucleic Acids Res. 1994 Dec 11;22(24):5354–5359. doi: 10.1093/nar/22.24.5354. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Parvin J. D., McCormick R. J., Sharp P. A., Fisher D. E. Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor. Nature. 1995 Feb 23;373(6516):724–727. doi: 10.1038/373724a0. [DOI] [PubMed] [Google Scholar]
  22. 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 Jul 14;82(1):143–153. doi: 10.1016/0092-8674(95)90060-8. [DOI] [PubMed] [Google Scholar]
  23. Stöver T., Köhler E., Fagin U., Wende W., Wolfes H., Pingoud A. Determination of the DNA bend angle induced by the restriction endonuclease EcoRV in the presence of Mg2+. J Biol Chem. 1993 Apr 25;268(12):8645–8650. [PubMed] [Google Scholar]
  24. Thompson J. F., Landy A. Empirical estimation of protein-induced DNA bending angles: applications to lambda site-specific recombination complexes. Nucleic Acids Res. 1988 Oct 25;16(20):9687–9705. doi: 10.1093/nar/16.20.9687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Walder R. Y., Walder J. A., Donelson J. E. The organization and complete nucleotide sequence of the PstI restriction-modification system. J Biol Chem. 1984 Jun 25;259(12):8015–8026. [PubMed] [Google Scholar]
  26. Wu H. M., Crothers D. M. The locus of sequence-directed and protein-induced DNA bending. Nature. 1984 Apr 5;308(5959):509–513. doi: 10.1038/308509a0. [DOI] [PubMed] [Google Scholar]
  27. Wu J. C., Santi D. V. Kinetic and catalytic mechanism of HhaI methyltransferase. J Biol Chem. 1987 Apr 5;262(10):4778–4786. [PubMed] [Google Scholar]
  28. Zahn K., Blattner F. R. Direct evidence for DNA bending at the lambda replication origin. Science. 1987 Apr 24;236(4800):416–422. doi: 10.1126/science.2951850. [DOI] [PubMed] [Google Scholar]

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