Proteomics

Dataset Information

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BMAL1 associates with NOP58 in the nucleolus and contributes to pre-rRNA processing


ABSTRACT: The transcription factor BMAL1 is a core element of the circadian clock that contributes to cyclic control of genes transcribed by RNA polymerase II. By using biochemical cellular fractionation and immunofluorescence analyses we reveal a previously uncharacterized nucleolar localization for BMAL1. We used an unbiased approach to determine the BMAL1 interactome by mass spectrometry and identified NOP58 as a prominent nucleolar interactor. NOP58, a core component of the box C/D small nucleolar ribonucleoprotein complex, associates with Snord118 to control specific pre-ribosomal RNA (rRNA) processing steps. These results suggest a non-canonical role of BMAL1 in rRNA regulation. Indeed, we show that BMAL1 controls NOP58-associated Snord118 nucleolar levels and cleavage of unique pre-rRNA intermediates. Our findings identify an unsuspected function of BMAL1 in the nucleolus that appears distinct from its canonical role in the circadian clock system

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Liver

SUBMITTER: Ignasi Forne  

LAB HEAD: Paolo Sassone-Corsi

PROVIDER: PXD018946 | Pride | 2020-08-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Ref560_MC_20160202_01.raw Raw
Ref560_MC_20160202_02.raw Raw
Ref560_MC_20160202_03.raw Raw
Ref560_MC_20160202_04.raw Raw
Ref560_MC_20160202_05.raw Raw
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Publications

BMAL1 Associates with NOP58 in the Nucleolus and Contributes to Pre-rRNA Processing.

Cervantes Marlene M   Forné Ignasi I   Ranjit Suman S   Gratton Enrico E   Imhof Axel A   Sassone-Corsi Paolo P  

iScience 20200512 6


The transcription factor BMAL1 is a core element of the circadian clock that contributes to cyclic control of genes transcribed by RNA polymerase II. By using biochemical cellular fractionation and immunofluorescence analyses we reveal a previously uncharacterized nucleolar localization for BMAL1. We used an unbiased approach to determine the BMAL1 interactome by mass spectrometry and identified NOP58 as a prominent nucleolar interactor. NOP58, a core component of the box C/D small nucleolar rib  ...[more]

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