Sharing of mitotic pre-ribosomal particles between daughter cells

Sirri, Valentina; Jourdan, Nathalie; Hernandez‐Verdun, Danièle; Roussel, Pascal

doi:10.1242/jcs.180521

Cited by 25 publications

(32 citation statements)

References 38 publications

(69 reference statements)

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“…Indeed, inhibition of pre-rRNA transcription with ActD retarded iPNB disassembly, although pre-rRNA processing was not substantially altered. These results are in agreement with the data of Roussel and colleagues, who demonstrated that processing of pre-rRNA is not sufficient to induce disappearance of PNBs, which appears to require the presence of functional nucleoli (Sirri et al, 2016). Further studies are necessary to confirm our hypothesis.…”

Section: Discussionsupporting

confidence: 93%

RNA-dependent disassembly of nuclear bodies

Musinova

Lisitsyna

Sorokin

et al. 2016

Journal of Cell Science

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Nuclear bodies are membraneless organelles that play important roles in genome functioning. A specific type of nuclear bodies known as interphase prenucleolar bodies (iPNBs) are formed in the nucleoplasm after hypotonic stress from partially disassembled nucleoli. iPNBs are then disassembled, and the nucleoli are reformed simultaneously. Here, we show that diffusion of B23 molecules (also known as nucleophosmin, NPM1) from iPNBs, but not fusion of iPNBs with the nucleoli, contributes to the transfer of B23 from iPNBs to the nucleoli. Maturation of pre-ribosomal RNAs (rRNAs) and the subsequent outflow of mature rRNAs from iPNBs led to the disassembly of iPNBs. We found that B23 transfer was dependent on the synthesis of pre-rRNA molecules in nucleoli; these pre-rRNA molecules interacted with B23 and led to its accumulation within nucleoli. The transfer of B23 between iPNBs and nucleoli was accomplished through a nucleoplasmic pool of B23, and increased nucleoplasmic B23 content retarded disassembly, whereas B23 depletion accelerated disassembly. Our results suggest that iPNB disassembly and nucleolus assembly might be coupled through RNA-dependent exchange of nucleolar proteins, creating a highly dynamic system with long-distance correlations between spatially distinct processes.

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Section: Discussionsupporting

confidence: 93%

RNA-dependent disassembly of nuclear bodies

Musinova

Lisitsyna

Sorokin

et al. 2016

Journal of Cell Science

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“…The proteins with a later recruitment could facilitate the assembly of the nucleolus during mitotic exit. Previous studies show that pre-nucleolar bodies are formed on the chromosomal periphery during telophase (Savino et al, 2001;Angelier et al, 2005;Sirri et al, 2016). Proteins showing a late chromosomal recruitment might hence be needed for the early reformation of the nucleolus after cell division.…”

Section: Discussionmentioning

confidence: 95%

Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder

Stenström

Mahdessian

Gnann

et al. 2020

Preprint

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The nucleolus is essential for ribosome biogenesis, but also involved in many other cellular functions. We performed a systematic spatiotemporal dissection of the human nucleolar proteome using confocal microscopy. In total, 1318 nucleolar proteins were identified; 287 localized to fibrillar components, and 157 were enriched along the nucleoplasmic border, indicating a unique proteome composition in this phase-separated region. We identified 65 nucleolar proteins (36 unknown) to relocate to the chromosomal periphery during mitosis.Interestingly, we here observed a temporal partitioning into two phenotypes; early (prometaphase), or late (after metaphase) recruitment, suggesting phase specific functions.We further show that expression of MKI67 is critical for this temporal partitioning. We provide the first proteome-wide analysis of intrinsic protein disorder for an organelle, and show that nucleolar proteins in general, and mitotic chromosome proteins in particular, have significantly higher intrinsic disorder level compared to cytosolic proteins, indicating that the perichromosomal layer is liquid-like. In summary, this study provides a comprehensive and essential resource of spatiotemporal expression data for the nucleolar proteome as part of the Human Protein Atlas.

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“…PCRs and/or real-time qPCRs were performed using oligonucleotides corresponding to human rDNA (Sirri et al, 2016). The forward oligonucleotides were: ETS1, 5′-GAGGTTGGGCCTCCGGATGC-3′; ETS3, 5′-CCTCTGACGCGGCAGACAGC-3′; ETS5, 5′-GTCGGTGTG-GGGTTCGAGGC-3′; 5.8S1, 5′-CACTTCGAACGCACTTGCGG-3′; and 18S1, 5′-GTTCAAAGCAGGCCCGAGCC-3′.…”

Section: Primersmentioning

confidence: 99%

“…The ETS (nt +935 to +1082) and 5.8S+ (nt +6718 to +6845, numbers given relative to the transcription start site defined as the +1 position) probes corresponding to fragments of human rDNA were generated as digoxigeninlabeled using primers ETS5 and ETS6 and primers 5.8S1 and 5.8S2, respectively, and the PCR DIG probe synthesis kit (Roche, Sirri et al, 2016).…”

Section: Probesmentioning

confidence: 99%

Sirtuin 7 promotes 45S pre-rRNA cleavage at site 2 and determines the processing pathway

Sirri

Grob

Berthelet

et al. 2019

Journal of Cell Science

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In humans, ribosome biogenesis mainly occurs in nucleoli following two alternative pre-rRNA processing pathways differing in the order in which cleavages take place but not by the sites of cleavage. To uncover the role of the nucleolar NAD +-dependent deacetylase sirtuin 7 in the synthesis of ribosomal subunits, pre-rRNA processing was analyzed after sirtinol-mediated inhibition of sirtuin 7 activity or depletion of sirtuin 7 protein. We thus reveal that sirtuin 7 activity is a critical regulator of processing of 45S, 32S and 30S pre-rRNAs. Sirtuin 7 protein is primarily essential to 45S pre-rRNA cleavage at site 2, which is the first step of processing pathway 2. Furthermore, we demonstrate that sirtuin 7 physically interacts with Nop56 and the GAR domain of fibrillarin, and propose that this could interfere with fibrillarin-dependent cleavage. Sirtuin 7 depletion results in the accumulation of 5′ extended forms of 32S pre-rRNA, and also influences the localization of fibrillarin. Thus, we establish a close relationship between sirtuin 7 and fibrillarin, which might determine the processing pathway used for ribosome biogenesis.

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Sharing of mitotic pre-ribosomal particles between daughter cells

Cited by 25 publications

References 38 publications

RNA-dependent disassembly of nuclear bodies

RNA-dependent disassembly of nuclear bodies

Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder

Sirtuin 7 promotes 45S pre-rRNA cleavage at site 2 and determines the processing pathway

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