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Article Dans Une Revue Biochemical Journal Année : 1994

Archaebacterial histone-like protein MC1 can exhibit a sequence-specific binding to DNA

Résumé

The binding of MC1 protein, the major chromosomal protein of the archaebacterium Methanosarcina sp. CHTI 55, to the region proceeding the strongly expressed genes encoding methyl co-enzyme reductase in a closely related micro-organism has been investigated. By gel retardation and DNAase I footprinting assays, we identified a preferential binding sequence in a open reading frame of unknown function. The large area of DNA protected against DNAase I is interrupted by a strong cleavage enhancement site on each strand. By circular permutation assays, we showed that the DNA bends upon MC1 binding. Furthermore we observed that the presence of a sequence outside the binding site can induce an unusual electrophoretic behaviour in some complexes.
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Dates et versions

hal-02708673 , version 1 (01-06-2020)

Identifiants

  • HAL Id : hal-02708673 , version 1
  • PRODINRA : 11208

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Caroline Teyssier, Bernard Lainé, Alain Gervais, Jean-Claude Maurizot, Francoise Culard. Archaebacterial histone-like protein MC1 can exhibit a sequence-specific binding to DNA. Biochemical Journal, 1994, 303 (2), pp.567-573. ⟨hal-02708673⟩
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