Structural modularity of the XIST ribonucleoprotein complex

Zhipeng Lu; Jimmy K. Guo; Yuning Wei; Diana R. Dou; Brian Zarnegar; Qing Ma; Rui Li; Yang Zhao; Fan Liu; Hani Choudhry; Paul A. Khavari; Howard Y. Chang

doi:10.1038/s41467-020-20040-3

Nature Communications (Dec 2020)

Structural modularity of the XIST ribonucleoprotein complex

Zhipeng Lu,
Jimmy K. Guo,
Yuning Wei,
Diana R. Dou,
Brian Zarnegar,
Qing Ma,
Rui Li,
Yang Zhao,
Fan Liu,
Hani Choudhry,
Paul A. Khavari,
Howard Y. Chang

Affiliations

Zhipeng Lu: Center for Personal Dynamic Regulomes, Stanford University
Jimmy K. Guo: Center for Personal Dynamic Regulomes, Stanford University
Yuning Wei: Center for Personal Dynamic Regulomes, Stanford University
Diana R. Dou: Center for Personal Dynamic Regulomes, Stanford University
Brian Zarnegar: Department of Dermatology, Stanford University School of Medicine
Qing Ma: Center for Personal Dynamic Regulomes, Stanford University
Rui Li: Center for Personal Dynamic Regulomes, Stanford University
Yang Zhao: Center for Personal Dynamic Regulomes, Stanford University
Fan Liu: Center for Personal Dynamic Regulomes, Stanford University
Hani Choudhry: Center for Personal Dynamic Regulomes, Stanford University
Paul A. Khavari: Department of Dermatology, Stanford University School of Medicine
Howard Y. Chang: Center for Personal Dynamic Regulomes, Stanford University

DOI: https://doi.org/10.1038/s41467-020-20040-3
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 14

Abstract

Read online

The long noncoding RNA XIST plays a central role in sex-specific gene expression in humans by silencing one of two X chromosomes in female cells. Here the authors show that higher order secondary structure creates the modular domain structure of XIST ribonucleoprotein complex and spatial separation of functions.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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