A comprehensive Xist interactome reveals cohesin repulsion and an RNA-directed chromosome conformation

Author:

Minajigi Anand1,Froberg John E.1,Wei Chunyao1,Sunwoo Hongjae1,Kesner Barry1,Colognori David1,Lessing Derek1,Payer Bernhard1,Boukhali Myriam2,Haas Wilhelm2,Lee Jeannie T.1

Affiliation:

1. Howard Hughes Medical Institute; Department of Molecular Biology, Massachusetts General Hospital, Boston, MA, USA; Department of Genetics, Harvard Medical School, Boston, MA, USA.

2. Massachusetts General Hospital Cancer Center, Charlestown, Boston, MA; Department of Medicine, Harvard Medical School, Boston, MA, USA.

Abstract

Protein partners for chromosome silencing Female mammals have two X chromosomes, one of which is almost completely shut down during development. The long noncoding Xist RNA plays a role in this process. To understand how a whole chromosome can be stably inactivated, Minajigi et al. identified many of the proteins that bind to the Xist RNA, which include cohesins. Paradoxically, the interaction between Xist and cohesin subunits resulted in repulsion of cohesin complexes from the inactive X chromosome, changing the three-dimensional shape of the whole chromosome. Science , this issue 10.1126/science.aab2276

Funder

National Science Foundation

NIH

HHMI

International Rett Syndrome Foundation

Rett Syndrome Research Trust

MGH Fund for Medical Discovery

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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