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Article Dans Une Revue Biomolecular NMR Assignments Année : 2015

Chemical shifts assignments of the archaeal MC1 protein and a strongly bent 15 base pairs DNA duplex in complex

Karine Loth
Céline Landon
Françoise Paquet

Résumé

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, 1H 15N MC1 protein and 1H 13C 15N bent duplex DNA, as first step towards the first experimental 3D structure of this new type of DNA/protein complex.
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Dates et versions

hal-01171478 , version 1 (03-07-2015)

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Karine Loth, Céline Landon, Françoise Paquet. Chemical shifts assignments of the archaeal MC1 protein and a strongly bent 15 base pairs DNA duplex in complex. Biomolecular NMR Assignments, 2015, 9 (1), pp.215-217. ⟨10.1007/s12104-014-9577-8⟩. ⟨hal-01171478⟩
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