The nucleolus: a site of ribonucleoprotein maturation

Gerbi, Susan A.; Borovjagin, Anton V.; Lange, Thilo S.

doi:10.1016/s0955-0674(03)00049-8

Cited by 109 publications

(87 citation statements)

References 52 publications

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“…The biogenesis of spliceosomal U snRNPs is a complicated process with multiple maturation steps that take place in a variety of subcellular compartments (reviewed in Carmo-Fonseca 2002b;Gerbi et al 2003;Will and Luhrmann 2001). With the exception of the U6 RNA, the spliceosomal small nuclear RNAs (snRNAs) are synthesized by RNA polymerase II as immature precursors containing a 5′-monomethyl cap and extra nucleotides at the 3′-end.…”

Section: Introductionmentioning

confidence: 99%

“…With the exception of the U6 RNA, the spliceosomal small nuclear RNAs (snRNAs) are synthesized by RNA polymerase II as immature precursors containing a 5′-monomethyl cap and extra nucleotides at the 3′-end. The RNA is then transported to the cytoplasm, possibly after visits to the CB and/or nucleolus (Gerbi et al 2003;Will and Luhrmann 2001). In the cytoplasm, a structural motif (called the Sm-binding site) within the snRNA is bound by a septet of Sm proteins (B/B′, D1, D2, D3, E, F, G) in an ordered manner that is regulated by the survival of motor neurons (SMN) protein complex.…”

Section: Introductionmentioning

confidence: 99%

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The C-terminal domain of coilin interacts with Sm proteins and U snRNPs

Pillai

Azzouz

et al. 2005

Chromosoma

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Coilin is the signature protein of the Cajal body (CB), a nuclear suborganelle involved in the biogenesis of small nuclear ribonucleoproteins (snRNPs). Newly imported Sm-class snRNPs are thought to traffic through CBs before proceeding to their final nuclear destinations. Loss of coilin function in mice leads to significant viability and fertility problems. Coilin interacts directly with the spinal muscular atrophy (SMA) protein via dimethylarginine residues in its C-terminal domain. Although coilin hypomethylation results in delocalization of survival of motor neurons (SMN) from CBs, high concentrations of snRNPs remain within these structures. Thus, CBs appear to be involved in snRNP maturation, but factors that tether snRNPs to CBs have not been described. In this report, we demonstrate that the coilin C-terminal domain binds directly to various Sm and Lsm proteins via their Sm motifs. We show that the region of coilin responsible for this binding activity is separable from that which binds to SMN. Interestingly, U2, U4, U5, and U6 snRNPs interact with the coilin C-terminal domain in a glutathione S-transferase (GST)-pulldown assay, whereas U1 and U7 snRNPs do not. Thus, the ability to interact with free Sm (and Lsm) proteins as well as with intact snRNPs, indicates that coilin and CBs may facilitate the modification of newly formed snRNPs, the regeneration of 'mature' snRNPs, or the reclamation of unassembled snRNP components.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The C-terminal domain of coilin interacts with Sm proteins and U snRNPs

Pillai

Azzouz

et al. 2005

Chromosoma

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“…In addition to its direct association with ribosome biogenesis, the nucleolus is also associated with or involved in other cell processes such as ageing, cancerogenesis, regulation of telomerase function and stabilization of the protein p53 (PED-ERSON 1998;SANTORO & GRUMMT 2001;OLSON et al 2002;GERBI et al 2003;RAŠKA et al 2006). There is also a direct relationship between the activity of nucleolar organizer regions and cell division (DERENZINI 1990;RAŠKA et al 2006).…”

Section: Discussionmentioning

confidence: 99%

Age-Dependent Change in the Morphology of Nucleoli and Methylation of Genes of the Nucleolar Organizer Region in Japanese Quail (<I>Coturnix japonica</I>) Model (Temminck and Schlegel, 1849) (Galliformes: Aves)

Andraszek¹,

Gryzińska²,

Wójcik³

et al. 2014

folia biol (krakow)

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ANDRASZEK K., GRYZIÑSKA M., WÓJCIK E., KNAGA S., SMALEC E. 2014. Age-dependent change in the morphology of nucleoli and methylation of genes of the nucleolar organizer region in Japanese quail (Coturnix japonica) model (Temminck and Schlegel, 1849) (Galliformes: Aves). Folia Biologica (Kraków) $ : 293-300. Nucleoli are the product of the activity of nucleolar organizer regions (NOR) in certain chromosomes. Their main functions are the formation of ribosomal subunits from ribosomal protein molecules and the transcription of genes encoding rRNA. The aim of the study was to determine the shape of nucleoli and analyse methylation in the gene RN28S in the spermatocytes of male Japanese quail (Coturnix japonica) in two age groups. Nucleoli were analysed in cells of the first meiotic prophase. Their number and shape were determined and they were classified as regular, irregular or defragmented. In the cells of the young birds no defragmented nucleoli were observed, with regular and irregular nucleoli accounting for 97% and 3%, respectively. In the cells of older birds no regular nucleoli were observed, while irregular and defragmented nucleoli accounted for 37% and 67%, respectively. MSP (methylation-specific PCR) showed that the gene RN28S is methylated in both 15-week-old and 52-week-old quails. In recent years an association has been established between nucleolus morphology and cellular ageing processes.

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“…These ancillary molecules associate and dissociate from pre-ribosome and pre-ribosomal subunits during their movement from the nucleolus (the site of primary assembly) via the nucleus, to their final destination in the cytoplasm [1]. Different steps of pre-ribosome maturation have been elucidated in recent years (reviewed in [1][2][3][4][5][6][7][8][9][10][11]), but some intriguing aspects of these processes remain unclear. Among these, two important questions that remain are: (1) why the two ribosomal sub-units have different fates during maturation, and (2) why the different steps in the ribosomal particle maturation occur in different cellular compartments.…”

Section: Introductionmentioning

confidence: 99%

“…The opening events of ribosome biogenesis occur in the nucleolus [4,8,12] where a newly synthesized polycistronic rRNA transcript (indicated as 35S in yeast, the organism in which this process has been extensively studied) is complexed with RP to form the 90S pre-ribosome [7,13]. The 35S rRNA primary precursor is cotranscriptionally processed at 3 0 end by an endonuclease (RntI) [10,14] which removes a large part of the 3 0 -external transcribed spacer (3 0 -ETS).…”

Section: Introductionmentioning

confidence: 99%

Evidence for a novel cytoplasmic processing event in ribosome maturation in the sea urchin Paracentrotus lividus

Bellavia

Barbieri

2010

Cell. Mol. Life Sci.

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In this paper we demonstrate the existence of a cytoplasmic processing step, never before described, involving both the pre-ribosomal subunits in the sea urchin Paracentrotus lividus. Northern-blot hybridization, primer extension, S1 mapping experiments and in situ hybridizations allowed us to demonstrate that cytoplasmic processed particles are successively re-imported into the nucleus where maturation of their RNAs is completed prior to being exported to the cytoplasm. Our findings lead to the proposal of a new model of ribosome maturation and shuttling.

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The nucleolus: a site of ribonucleoprotein maturation

Cited by 109 publications

References 52 publications

The C-terminal domain of coilin interacts with Sm proteins and U snRNPs

The C-terminal domain of coilin interacts with Sm proteins and U snRNPs

Age-Dependent Change in the Morphology of Nucleoli and Methylation of Genes of the Nucleolar Organizer Region in Japanese Quail (<I>Coturnix japonica</I>) Model (Temminck and Schlegel, 1849) (Galliformes: Aves)

Evidence for a novel cytoplasmic processing event in ribosome maturation in the sea urchin Paracentrotus lividus

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