title: Chemical shifts assignments of the archaeal MC1 protein and a strongly bent 15 base pairs DNA duplex in complex.
abstract: MC1 is the most abundant architectural protein present in Methanosarcina thermophila CHTI55 in laboratory growth conditions and is structurally unrelated to other DNA-binding proteins. MC1 functions are to shape and to protect DNA against thermal denaturation by binding to it. Therefore, MC1 has a strong affinity for any double-stranded DNA. However, it recognizes and preferentially binds to bent DNA, such as four-way junctions and negatively supercoiled DNA minicircles. Combining NMR data, electron microscopy data, biochemistry, molecular modelisation and docking approaches, we proposed recently a new type of DNA/protein complex, in which the monomeric protein MC1 binds on the concave side of a strongly bent 15 base pairs DNA. We present here the NMR chemical shifts assignments of each partner in the complex, (1)H (15)N MC1 protein and (1)H (13)C (15)N bent duplex DNA, as first step towards the first experimental 3D structure of this new type of DNA/protein complex.
authors.affiliation: Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
authors.forename: Karine
authors.initials: K
authors.lastname: Loth
authors.forename: Céline
authors.initials: C
authors.lastname: Landon
authors.forename: Françoise
authors.initials: F
authors.lastname: Paquet
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D020029:Base Pairing; D019641:DNA, Archaeal / Q000737:chemistry* / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D017020:Methanosarcina; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding
chemical_list: D019843:Archaeal Proteins; D019641:DNA, Archaeal; D004268:DNA-Binding Proteins