caa a22 4500 445325135 CHVBK 20180317142717.0 cr unu---uuuuu 170323e20111101xx s 000 0 eng 10.1007/s10858-011-9555-8 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9555-8 Marius Clore G. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 02892-0520, Bethesda, MD, USA aut Exploring translocation of proteins on DNA by NMR [Elektronische Daten] [G. Marius Clore] While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcription factors locate their specific DNA target site within an overwhelming sea of non-specific DNA sites. Indirect kinetic data suggested that three processes are involved in the search procedure: jumping by dissociation of the protein from the DNA followed by re-association at another site, direct transfer from one DNA molecule or segment to another, and one-dimensional sliding. In this brief perspective I summarize recent NMR developments from our laboratory that have permitted direct characterization of the species and molecular mechanisms involved in the target search process, including the detection of highly transient sparsely-populated states. The main tool in these studies involves the application of paramagnetic relaxation enhancement, supplemented by z-exchange spectroscopy, lineshape analysis and residual dipolar couplings. These studies led to the first direct demonstration of rotation-coupled sliding of a protein along the DNA and the direct transfer of a protein from one DNA molecule to another without dissociating into free solution. Springer Science+Business Media B.V. (outside the USA), 2011 Protein-DNA interactions nationallicence Sliding nationallicence Direct transfer nationallicence Target search process nationallicence Paramagnetic relaxation enhancement nationallicence z -Exchange spectroscopy nationallicence Lineshape analysis nationallicence Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 209-219 0925-2738 51:3<209 2011 51 10858 https://doi.org/10.1007/s10858-011-9555-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9555-8 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Marius Clore G. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 02892-0520, Bethesda, MD, USA aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 209-219 0925-2738 51:3<209 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer