Journal
JOURNAL OF CELL BIOLOGY
Volume 219, Issue 11, Pages -Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201910148
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Funding
- Center for the Study of Inflammatory Bowel Disease grant [DK043351]
- Boston Area Diabetes and Endocrinology Research Center award [DK057521]
- National Institutes of Health [1S10 RR031563-01, GM122893]
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During mitosis, the genome is transformed from a decondensed, transcriptionally active state to a highly condensed, transcriptionally inactive state. Mitotic chromosome reorganization is marked by the general attenuation of transcription on chromosome arms, yet how the cell regulates nuclear and chromatin-associated RNAs after chromosome condensation and nuclear envelope breakdown is unknown. SAF-A/hnRNPU is an abundant nuclear protein with RNA-to-DNA tethering activity, coordinated by two spatially distinct nucleic acid-binding domains. Here we show that RNA is evicted from prophase chromosomes through Aurora-B-dependent phosphorylation of the SAF-A DNA-binding domain; failure to execute this pathway leads to accumulation of SAF-A-RNA complexes on mitotic chromosomes, defects in metaphase chromosome alignment, and elevated rates of chromosome missegregation in anaphase. This work reveals a role for Aurora-B in removing chromatin-associated RNAs during prophase and demonstrates that Aurora-B-dependent relocalization of SAF-A during cell division contributes to the fidelity of chromosome segregation.
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