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Structural Insights into Nonspecific Binding of DNA by TrmBL2, an Archaeal Chromatin Protein

Structural Insights into Nonspecific Binding of DNA by TrmBL2, an Archaeal Chromatin Protein

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Prüfsumme: MD5:571fd4f51588dbbabc19c2e96b8f9e81

AHMAD, Misbha Ud Din, Ingrid WAEGE, Winfried HAUSNER, Michael THOMM, Winfried BOOS, Kay DIEDERICHS, Wolfram WELTE, 2015. Structural Insights into Nonspecific Binding of DNA by TrmBL2, an Archaeal Chromatin Protein. In: Journal of Molecular Biology. 427(20), pp. 3216-3229. ISSN 0022-2836. eISSN 1089-8638. Available under: doi: 10.1016/j.jmb.2015.08.012

@article{Ahmad2015-10-09Struc-31791, title={Structural Insights into Nonspecific Binding of DNA by TrmBL2, an Archaeal Chromatin Protein}, year={2015}, doi={10.1016/j.jmb.2015.08.012}, number={20}, volume={427}, issn={0022-2836}, journal={Journal of Molecular Biology}, pages={3216--3229}, author={Ahmad, Misbha Ud Din and Waege, Ingrid and Hausner, Winfried and Thomm, Michael and Boos, Winfried and Diederichs, Kay and Welte, Wolfram} }

Thomm, Michael Waege, Ingrid Diederichs, Kay 2015-09-21T11:38:47Z Boos, Winfried Ahmad, Misbha Ud Din Hausner, Winfried 2015-10-09 eng Hausner, Winfried The crystal structure of TrmBL2 from the archaeon Pyrococcus furiosus shows an association of two pseudosymmetric dimers. The dimers follow the prototypical design of known bacterial repressors with two helix–turn–helix (HTH) domains binding to successive major grooves of the DNA. However, in TrmBL2, the two dimers are arranged at a mutual displacement of approximately 2 bp so that they associate with the DNA along the double-helical axis at an angle of approximately 80°.<br /><br />While the deoxyribose phosphate groups of the double-stranded DNA (dsDNA) used for co-crystallization are clearly seen in the electron density map, most of the nucleobases are averaged out. Refinement required to assume a superposition of at least three mutually displaced dsDNAs. The HTH domains interact primarily with the deoxyribose phosphate groups and polar interactions with the nucleobases are almost absent.<br /><br />This hitherto unseen mode of DNA binding by TrmBL2 seems to arise from nonoptimal protein–DNA contacts made by its four HTH domains resulting in a low-affinity, nonspecific binding to DNA. 2015-09-21T11:38:47Z Welte, Wolfram Diederichs, Kay Welte, Wolfram Ahmad, Misbha Ud Din Boos, Winfried Thomm, Michael Waege, Ingrid Structural Insights into Nonspecific Binding of DNA by TrmBL2, an Archaeal Chromatin Protein

Dateiabrufe seit 21.09.2015 (Informationen über die Zugriffsstatistik)

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