NMR studies of DNA support the role of pre-existing minor groove variations in nucleosome indirect readout.
Biochemistry. 2014 Aug 7;
Authors: Xu X, Ben Imeddourene A, Zargarian L, Foloppe N, Mauffret O, Hartmann B
Abstract
We investigated how the intrinsic sequence-dependent properties probed via the phosphate linkages (BI BII equilibrium) influence the preferred shape of free DNA, and how this affects the nucleosome formation. First, this exploits NMR solution studies of four B-DNA dodecamers that together cover 39 base pairs of the 5' half of the sequence 601, of special interest for nucleosome formation. The results validate our previous prediction of a systematic, general sequence effect on the intrinsic backbone BII propensities. NMR provides new evidence that the backbone behavior is intimately coupled to the minor groove width. Second, application of the backbone behavior predictions to the full sequence 601 and other relevant sequences demonstrates that alternation of intrinsic low and high BII propensities, coupled to intrinsic narrow and wide minor grooves, largely coincides with the sinusoidal variations of the DNA minor groove width observed in crystallographic structures of the nucleosome. This correspondence is much poorer with low affinity sequences. Overall, the results indicate that nucleosome formation involves an indirect readout process implicating pre-existing DNA minor groove conformations. It also illustrates how the prediction of the intrinsic structural DNA behavior offers a powerful framework to gain explanatory insight on how proteins read DNA.
PMID: 25102280 [PubMed - as supplied by publisher]
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Abstract
A description of the utility of deuteration in protein NMR is provided with an emphasis on quantitative evaluation of the effects of deuteration on a number of NMR parameters of proteins: (1) chemical shifts, (2) scalar coupling constants, (3) relaxation...
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Indirect Use of Deuterium in Solution NMR Studies of Protein Structure and Hydrogen Bonding
Indirect Use of Deuterium in Solution NMR Studies of Protein Structure and Hydrogen Bonding
Publication date: Available online 28 August 2013
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Vitali Tugarinov</br>
A description of the utility of deuteration in protein NMR is provided with an emphasis on quantitative evaluation of the effects of deuteration on a number of NMR parameters of proteins: (1) chemical shifts, (2) scalar coupling constants, (3) relaxation properties (R 1 and R 2 rates) of nuclei directly attached to one or more...
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
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Major groove width variations in RNA structures determined by NMR and impact of 13C r
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