Open AccessArchaebacterial histone-like protein MC1 can exhibit a sequence-specific binding to DNA
Author(s) -
Caroline Teyssier,
Bernard Lainé,
Alain Gervais,
JeanClaude Maurizot,
Françoise Culard
Publication year - 1994
Publication title -
biochemical journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.706
H-Index - 265
eISSN - 1470-8728
pISSN - 0264-6021
DOI - 10.1042/bj3030567
Subject(s) - biology , dna , footprinting , binding site , dna footprinting , microbiology and biotechnology , genetics , dna binding protein , gene , biochemistry , base sequence , transcription factor
The binding of MC1 protein, the major chromosomal protein of the archaebacterium Methanosarcina sp. CHTI 55, to the region preceding the strongly expressed genes encoding methyl coenzyme 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 an 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.