2fj7

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2fj7, resolution 3.2Å

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Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element

Overview

Poly(dA.dT) DNA sequence elements are thought to promote transcription by, either excluding nucleosomes or by altering their structural or dynamic, properties. Here, the stability and structure of a defined nucleosome core, particle containing a 16 base-pair poly(dA.dT) element (A16 NCP) was, investigated. The A16 NCP requires a significantly higher temperature for, histone octamer sliding in vitro compared to comparable nucleosomes that, do not contain a poly(dA.dT) element. Fluorescence resonance energy, transfer showed that the interactions between the nucleosomal DNA ends and, the histone octamer were destabilized in A16 NCP. The crystal structure of, A16 NCP was determined to a resolution of 3.2 A. The overall structure was, maintained except for local deviations in DNA conformation. These results, are consistent with previous in vivo and in vitro observations that, poly(dA.dT) elements cause only modest changes in DNA accessibility and, modest increases in steady-state transcription levels.

About this Structure

2FJ7 is a Protein complex structure of sequences from Xenopus laevis. Full crystallographic information is available from OCA.

Reference

Nucleosome core particles containing a poly(dA.dT) sequence element exhibit a locally distorted DNA structure., Bao Y, White CL, Luger K, J Mol Biol. 2006 Aug 25;361(4):617-24. Epub 2006 Jul 5. PMID:16860337

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