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Title: The lupus autoantigen La/Ssb is an Xist-binding protein involved in Xist folding and cloud formation
Authors: Ha, Norbert
Ding, Nan
Hong, Ru
Liu, Rubing
Roca, Xavier
Luo, Yingyuan
Duan, Xiaowei
Wang, Xiao
Ni, Peiling
Wu, Haiyang
Zhang, Li-Feng
Chen, Lingyi
Keywords: Science::Biological sciences
Issue Date: 2021
Source: Ha, N., Ding, N., Hong, R., Liu, R., Roca, X., Luo, Y., Duan, X., Wang, X., Ni, P., Wu, H., Zhang, L. & Chen, L. (2021). The lupus autoantigen La/Ssb is an Xist-binding protein involved in Xist folding and cloud formation. Nucleic Acids Research, 49(20), 11596-11613.
Project: MOE2015-T2-1-093
Journal: Nucleic Acids Research
Abstract: Using the programmable RNA-sequence binding domain of the Pumilio protein, we FLAG-tagged Xist (inactivated X chromosome specific transcript) in live mouse cells. Affinity pulldown coupled to mass spectrometry was employed to identify a list of 138 candidate Xist-binding proteins, from which, Ssb (also known as the lupus autoantigen La) was validated as a protein functionally critical for X chromosome inactivation (XCI). Extensive XCI defects were detected in Ssb knockdown cells, including chromatin compaction, death of female mouse embryonic stem cells during in vitro differentiation and chromosome-wide monoallelic gene expression pattern. Live-cell imaging of Xist RNA reveals the defining XCI defect: Xist cloud formation. Ssb is a ubiquitous and versatile RNA-binding protein with RNA chaperone and RNA helicase activities. Functional dissection of Ssb shows that the RNA chaperone domain plays critical roles in XCI. In Ssb knockdown cells, Xist transcripts are unstable and misfolded. These results show that Ssb is critically involved in XCI, possibly as a protein regulating the in-cell structure of Xist.
ISSN: 0305-1048
DOI: 10.1093/nar/gkab1003
Schools: School of Biological Sciences 
Rights: © The Authors 2021. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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