Protein–nucleic acids interactions: new ways of connecting structure, dynamics and function
Molecular machines that act on nucleic acids, DNA and RNA are at the heart of the field of cellular information processing. A coherent description of the interactions involved in their assembly, activities and regulation affords a quantitative understanding of how transcription factors and DNA repair proteins find their unique targets among millions of nonspecific sequences and undamaged DNA bases, how the intricate choreography of DNA replication, recombination and repair and gene expression is regulated, how viral particles self-assemble and how chromosomes are organized inside living cells. These important questions are not easy to answer for the following reasons:(1) transactions between proteins and nucleic acids commonly involve extended surfaces with multiple interaction epitopes, and the resulting macromolecular assemblies are non-homogenous and dynamic; (2) the structures of multicomponent protein–DNA and protein–RNA complexes are often refractory to analysis by traditional...
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Conflict of interest
Maria Spies and Brian O. Smith declare that they have no conflicts of interest to declare.
- Belorusova AY, Osz J, Petoukhov MV, Peluso-Iltis C, Kieffer B, Svergun DI, Rochel N (2016) Solution behavior of the intrinsically disordered N-terminal domain of retinoid X receptor alpha in the context of the full-length protein. Biochemistry 55(12):1741–1748CrossRefPubMedPubMedCentralGoogle Scholar
- Hamatsu J, O'Donovan D, Tanaka T, Shirai T, Hourai Y, Mikawa T, Ikeya T, Mishima M, Boucher W, Smith BO, Laue ED, Shirakawa M, Ito Y (2013) High-resolution heteronuclear multidimensional NMR of proteins in living insect cells using a baculovirus protein expression system. J Am Chem Soc 135(5):1688–1691CrossRefPubMedGoogle Scholar
- Martinez-Zapien D, Delsuc MA, Trave G, Lutzing R, Rochette-Egly C, Kieffer B (2014) Production and characterization of a retinoic acid receptor RARgamma construction encompassing the DNA binding domain and the disordered N-terminal proline rich domain. Protein Expr Purif 95:113–120CrossRefPubMedGoogle Scholar