Structure of Nucleosomes, Chromatin, and RNA Polymerase-Promoter Complex as Revealed by DNA-Protein Cross-linking

  1. A.D. Mirzabekov,
  2. S.G. Bavykin,
  3. V.L. Karpov,
  4. O.V. Preobrazhenskaya,
  5. K.K. Ebralidze,
  6. V.M. Tuneev,
  7. A.F. Melnikova,
  8. E.G. Goguadze,
  9. A.A. Chenchick, and
  10. R.S. Beabealashvili
  1. Institute of Molecular Biology, USSR Academy of Sciences, Moscow 117984, USSR

This extract was created in the absence of an abstract.

Excerpt

For several years we have been engaged in studying the structures of different DNA complexes. First, we investigated the arrangement of ligands within the DNA grooves. Mirzabekov and Kolchinsky (1974) introduced the methylation of DNA with dimethyl sulfate within the minor and major grooves of the DNA double helix, as well as within single-stranded DNA regions, in order to test the binding within the DNA grooves and to measure DNA unwinding in DNA complexes with histones, protamines, lac repressor, antibiotics (for review, see Mirzabekov et al. 1978b), and RNA polymerase (Melnikova et al. 1978). Further development of this approach has led to the localization of purine bases in the lac operator interacting with the lac repressor from the side of the major and minor grooves (Gilbert et al. 1976).

In studying DNA-protein interactions, it is necessary to determine the primary organization of the complexes and the locations of binding sites...

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