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U bodies are cytoplasmic structures that contain uridine-rich small nuclear ribonucleoproteins and associate with P bodies.

ABSTRACT: Uridine-rich small nuclear ribonucleoproteins (U snRNPs) are involved in key steps of pre-mRNA processing in the nucleus of eukaryotic cells. U snRNPs are enriched in the nucleus in discrete organelles that include speckles, Cajal bodies, and histone locus bodies. However, most U snRNPs are assembled in the cytoplasm, not in the nucleus. Despite extensive biochemical information, little is known about the spatial organization of U snRNPs in the cytoplasm. Here we show that U snRNPs in Drosophila are concentrated in discrete cytoplasmic structures, which we call U bodies, because they contain the major U snRNPs. In addition to snRNPs, U bodies contain essential snRNP assembly factors, suggesting that U bodies are sites for assembly or storage of snRNPs before their import into the nucleus. U bodies invariably associate with P bodies, which are involved in RNA surveillance and decay. Genetic disruption of P body components affects the organization of U bodies, suggesting that the two cytoplasmic bodies may cooperate in regulating aspects of snRNP metabolism. The identification of U bodies provides an opportunity to correlate specific biochemical steps of snRNP biogenesis with structural features of the cytoplasm.

SUBMITTER: Liu JL

PROVIDER: S-EPMC1899408 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Periodic expression of Sm proteins parallels formation of nuclear Cajal bodies and cytoplasmic snRNP-rich bodies.

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Coiled bodies preferentially associate with U4, U11, and U12 small nuclear RNA genes in interphase HeLa cells but not with U6 and U7 genes.

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Project description:The Cajal body (CB) is a nuclear structure closely associated with import and biogenesis of small nuclear ribonucleoprotein particles (snRNPs). Here, we tested whether CBs also contain mature snRNPs and whether CB integrity depends on the ongoing snRNP splicing cycle. Sm proteins tagged with photoactivatable and color-maturing variants of fluorescent proteins were used to monitor snRNP behavior in living cells over time; mature snRNPs accumulated in CBs, traveled from one CB to another, and they were not preferentially replaced by newly imported snRNPs. To test whether CB integrity depends on the snRNP splicing cycle, two human orthologues of yeast proteins involved in distinct steps in spliceosome disassembly after splicing, hPrp22 and hNtr1, were depleted by small interfering RNA treatment. Surprisingly, depletion of either protein led to the accumulation of U4/U6 snRNPs in CBs, suggesting that reassembly of the U4/U6.U5 tri-snRNP was delayed. Accordingly, a relative decrease in U5 snRNPs compared with U4/U6 snRNPs was observed in CBs, as well as in nuclear extracts of treated cells. Together, the data show that particular phases of the spliceosome cycle are compartmentalized in living cells, with reassembly of the tri-snRNP occurring in CBs.

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Project description:Over the past decade, evidence has identified a link between protein aggregation, RNA biology, and a subset of degenerative diseases. An important feature of these disorders is the cytoplasmic or nuclear aggregation of RNA-binding proteins (RBPs). Redistribution of RBPs, such as the human TAR DNA-binding 43 protein (TDP-43) from the nucleus to cytoplasmic inclusions is a pathological feature of several diseases. Indeed, sporadic and familial forms of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration share as hallmarks ubiquitin-positive inclusions. Recently, the wide spectrum of neurodegenerative diseases characterized by RBPs functions' alteration and loss was collectively named proteinopathies. Here, we show that TBPH (TAR DNA-binding protein-43 homolog), the Drosophila ortholog of human TDP-43 TAR DNA-binding protein-43, interacts with the arcRNA hsr? and with hsr?-associated hnRNPs. Additionally, we found that the loss of the omega speckles remodeler ISWI (Imitation SWI) changes the TBPH sub-cellular localization to drive a TBPH cytoplasmic accumulation. Our results, hence, identify TBPH as a new component of omega speckles and highlight a role of chromatin remodelers in hnRNPs nuclear compartmentalization.

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