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The structural basis of histone variant H2A.Z-dependent chromatin regulation


EMSL Project ID
51192

Abstract

The structural integrity and structural-dynamics of chromatin is of fundamental importance to all eukaryotes during normal development. Key factors in many genome regulation pathways exert their function through modulating the hierarchical organization of chromatin. Due to the complexity of the chromatin system and the technical challenges, our understanding of these processes is mostly limited to the nucleosome level, the first layer of genome packaging. In this proposal, we will use an in vitro system to mimic the higher-order structure of chromatin to dissect the mechanism-of-action of a histone variant H2A.Z. By employing single-particle cryo-electron microscopy (EM) and traditional biochemistry, we aim to obtain the high-resolution cryo-EM structures of canonical and variant H2A.Z chromatin fibers respectively. The outcomes of our proposed studies are significant. It not only will provide key insights into how the essential variant H2A.Z mediate chromatin structure and function, but it will also address a critical knowledge gap in our understanding of the dual-function of H2A.Z in vivo.

Project Details

Start Date
2019-11-10
End Date
2020-08-10
Status
Closed

Team

Principal Investigator

Dongyan Tan
Institution
Stony Brook University

Team Members

Tyler Lewis
Institution
Stony Brook University

Theo Humphreys
Institution
Oregon Health & Science University

Related Publications

Abstract of paper presented at the 2020 virtual meeting on Epigenetics & Chromatin, September 15 - September 18, 2020