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Essential role for the SMN complex in the specificity of snRNP assembly (2002)

L. Pellizzoni ; J. Yong ; G. Dreyfuss

American Association for the Advancement of Science (AAAS)

In: Science. 298(5599): 1775-9. doi: 10.1126/science.1074962.

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Publication Date: 2002-12-03

Description: The Survival of Motor Neurons (SMN) protein, the product of the spinal muscular atrophy-determining gene, is part of a large macromolecular complex (SMN complex) that functions in the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs). Using cell extracts and purified components, we demonstrated that the SMN complex is necessary and sufficient to mediate the ATP-dependent assembly of the core of seven Sm proteins on uridine-rich, small nuclear ribonucleic acids (U snRNAs). In vitro experiments revealed strict requirements for ordered binding of the Sm proteins and the U snRNAs to the SMN complex. Importantly, the SMN complex is necessary to ensure that Sm cores assemble only on correct RNA targets and prevent their otherwise promiscuous association with other RNAs. Thus, the SMN complex functions as a specificity factor essential for the efficient assembly of Sm proteins on U snRNAs and likely protects cells from illicit, and potentially deleterious, nonspecific binding of Sm proteins to RNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pellizzoni, Livio -- Yong, Jeongsik -- Dreyfuss, Gideon -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1775-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459587" target="_blank"〉PubMed〈/a〉

Keywords: Adenosine Triphosphate/metabolism ; Carrier Proteins/metabolism ; Cell Extracts ; Cyclic AMP Response Element-Binding Protein ; DEAD Box Protein 20 ; DEAD-box RNA Helicases ; HeLa Cells ; Humans ; Kinetics ; Models, Biological ; Nerve Tissue Proteins/isolation & purification/*metabolism ; Nuclear Proteins/metabolism ; Oligoribonucleotides/metabolism ; Protein Binding ; RNA Helicases/metabolism ; RNA, Small Nuclear/*metabolism ; RNA-Binding Proteins ; Ribonucleoproteins, Small Nuclear/isolation & purification/*metabolism ; SMN Complex Proteins

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex (2001)

V. N. Kim ; N. Kataoka ; G. Dreyfuss

American Association for the Advancement of Science (AAAS)

In: Science. 293(5536): 1832-6. doi: 10.1126/science.1062829.

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Publication Date: 2001-09-08

Description: Nonsense-mediated messenger RNA (mRNA) decay, or NMD, is a critical process of selective degradation of mRNAs that contain premature stop codons. NMD depends on both pre-mRNA splicing and translation, and it requires recognition of the position of stop codons relative to exon-exon junctions. A key factor in NMD is hUpf3, a mostly nuclear protein that shuttles between the nucleus and cytoplasm and interacts specifically with spliced mRNAs. We found that hUpf3 interacts with Y14, a component of post-splicing mRNA-protein (mRNP) complexes, and that hUpf3 is enriched in Y14-containing mRNP complexes. The mRNA export factors Aly/REF and TAP are also associated with nuclear hUpf3, indicating that hUpf3 is in mRNP complexes that are poised for nuclear export. Like Y14 and Aly/REF, hUpf3 binds to spliced mRNAs specifically ( approximately 20 nucleotides) upstream of exon-exon junctions. The splicing-dependent binding of hUpf3 to mRNAs before export, as part of the complex that assembles near exon-exon junctions, allows it to serve as a link between splicing and NMD in the cytoplasm.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, V N -- Kataoka, N -- Dreyfuss, G -- 5 R01 GM37125.14/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1832-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546873" target="_blank"〉PubMed〈/a〉

Keywords: 3' Untranslated Regions/genetics/metabolism ; Active Transport, Cell Nucleus ; Cell Line ; Codon, Nonsense/*genetics ; DNA-Binding Proteins/genetics/metabolism ; Exons/*genetics ; Fungal Proteins/genetics/*metabolism ; Globins/genetics ; Humans ; Macromolecular Substances ; Models, Biological ; Precipitin Tests ; Protein Binding ; RNA Splicing/*genetics ; RNA, Messenger/genetics/metabolism ; RNA-Binding Proteins/genetics/*metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Ribonucleoproteins/chemistry/metabolism ; *Saccharomyces cerevisiae Proteins ; Substrate Specificity

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Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

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Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins (1991)

S. Pinol-Roma ; G. Dreyfuss

American Association for the Advancement of Science (AAAS)

In: Science. 253(5017): 312-4.

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Publication Date: 1991-07-19

Description: Heterogeneous nuclear RNAs and specific nuclear proteins form heterogeneous nuclear ribonucleoprotein complexes (hnRNPs), one of the most abundant components of the nucleus. In mitosis, as the nuclear envelope breaks down, hnRNPs disperse throughout the cell. At the end of mitosis, hnRNPs dissociate and their proteins are transported into the daughter cell nuclei separately. Some are transported immediately (early group), while others are transported later (late group). Transport of the late group appears to require transcription by RNA polymerase II, in that inhibitors of this polymerase cause the late proteins to remain in the cytoplasm. Thus, there are two modes, transcription-dependent and transcription-independent, for the transport of nuclear proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pinol-Roma, S -- Dreyfuss, G -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):312-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia 19104-6148.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857966" target="_blank"〉PubMed〈/a〉

Keywords: Cell Nucleus/*physiology/ultrastructure ; Dactinomycin/pharmacology ; HeLa Cells/cytology/physiology ; Heterogeneous-Nuclear Ribonucleoproteins ; Humans ; Mitosis ; Nuclear Envelope/physiology/ultrastructure ; RNA Polymerase II/antagonists & inhibitors/metabolism ; RNA, Heterogeneous Nuclear/metabolism ; Ribonucleoproteins/genetics/*metabolism ; *Transcription, Genetic/drug effects

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation (2010)

D. Kaida ; M. G. Berg ; I. Younis ; [et al.]

Nature Publishing Group (NPG)

In: Nature. 468(7324): 664-8. doi: 10.1038/nature09479.

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Publication Date: 2010-10-01

Description: In eukaryotes, U1 small nuclear ribonucleoprotein (snRNP) forms spliceosomes in equal stoichiometry with U2, U4, U5 and U6 snRNPs; however, its abundance in human far exceeds that of the other snRNPs. Here we used antisense morpholino oligonucleotide to U1 snRNA to achieve functional U1 snRNP knockdown in HeLa cells, and identified accumulated unspliced pre-mRNAs by genomic tiling microarrays. In addition to inhibiting splicing, U1 snRNP knockdown caused premature cleavage and polyadenylation in numerous pre-mRNAs at cryptic polyadenylation signals, frequently in introns near (〈5 kilobases) the start of the transcript. This did not occur when splicing was inhibited with U2 snRNA antisense morpholino oligonucleotide or the U2-snRNP-inactivating drug spliceostatin A unless U1 antisense morpholino oligonucleotide was also included. We further show that U1 snRNA-pre-mRNA base pairing was required to suppress premature cleavage and polyadenylation from nearby cryptic polyadenylation signals located in introns. These findings reveal a critical splicing-independent function for U1 snRNP in protecting the transcriptome, which we propose explains its overabundance.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2996489/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2996489/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaida, Daisuke -- Berg, Michael G -- Younis, Ihab -- Kasim, Mumtaz -- Singh, Larry N -- Wan, Lili -- Dreyfuss, Gideon -- Howard Hughes Medical Institute/ -- England -- Nature. 2010 Dec 2;468(7324):664-8. doi: 10.1038/nature09479. Epub 2010 Sep 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20881964" target="_blank"〉PubMed〈/a〉

Keywords: Base Pairing ; Base Sequence ; HeLa Cells ; Humans ; Introns/genetics ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Oligonucleotides, Antisense/genetics/metabolism/pharmacology ; *Polyadenylation/drug effects/genetics ; Pyrans/pharmacology ; RNA Precursors/genetics/*metabolism ; *RNA Splicing/drug effects/genetics ; RNA, Small Nuclear/genetics/metabolism ; Ribonucleoprotein, U1 Small Nuclear/antagonists & inhibitors/genetics/*metabolism ; Spiro Compounds/pharmacology

Print ISSN: 0028-0836

Electronic ISSN: 1476-4687

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Published by Nature Publishing Group (NPG)

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Conserved structures and diversity of functions of RNA-binding proteins (1994)

C. G. Burd ; G. Dreyfuss

American Association for the Advancement of Science (AAAS)

In: Science. 265(5172): 615-21.

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Publication Date: 1994-07-29

Description: In eukaryotic cells, a multitude of RNA-binding proteins play key roles in the posttranscriptional regulation of gene expression. Characterization of these proteins has led to the identification of several RNA-binding motifs, and recent experiments have begun to illustrate how several of them bind RNA. The significance of these interactions is reflected in the recent discoveries that several human and other vertebrate genetic disorders are caused by aberrant expression of RNA-binding proteins. The major RNA-binding motifs are described and examples of how they may function are given.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burd, C G -- Dreyfuss, G -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):615-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia 19104-6148.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036511" target="_blank"〉PubMed〈/a〉

Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Humans ; Molecular Sequence Data ; RNA-Binding Proteins/*chemistry/*physiology ; Ribonucleoproteins/chemistry ; Sequence Homology, Amino Acid

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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6

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Heterogeneous nuclear ribonucleoproteins: role in RNA splicing (1986)

Y. D. Choi ; P. J. Grabowski ; P. A. Sharp ; [et al.]

American Association for the Advancement of Science (AAAS)

In: Science. 231(4745): 1534-9.

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Publication Date: 1986-03-28

Description: Splicing in vitro of a messenger RNA (mRNA) precursor (pre-mRNA) is inhibited by a monoclonal antibody to the C proteins (anti-C) of the heterogeneous nuclear RNA (hnRNA)-ribonucleoprotein (hnRNP) particles. This antibody, 4F4, inhibits an early step of the reaction: cleavage at the 3' end of the upstream exon and the formation of the intron lariat. In contrast, boiled 4F4, or a different monoclonal antibody (designated 2B12) to the C proteins, or antibodies to other hnRNP proteins (120 and 68 kilodaltons) and nonimmune mouse antibodies have no inhibitory effect. The 4F4 antibody does not prevent the adenosine triphosphate-dependent formation of a 60S splicing complex (spliceosome). Furthermore, the 60S splicing complex contains C proteins, and it can be immunoprecipitated with 4F4. Depletion of C proteins from the splicing extract by immunoadsorption with either of the two monoclonal antibodies to the C proteins (4F4 or 2B12) results in the loss of splicing activity, whereas mock-depletion with nonimmune mouse antibodies bodies has no effect. A 60S splicing complex does not form in a C protein-depleted nuclear extract. These results indicate an essential role for proteins of the hnRNP complex in the splicing of mRNA precursors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, Y D -- Grabowski, P J -- Sharp, P A -- Dreyfuss, G -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1534-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3952495" target="_blank"〉PubMed〈/a〉

Keywords: Adenosine Triphosphate/metabolism ; Antibodies, Monoclonal/*immunology ; HeLa Cells ; Heterogeneous-Nuclear Ribonucleoproteins ; Humans ; In Vitro Techniques ; Macromolecular Substances ; *RNA Splicing ; RNA, Heterogeneous Nuclear/metabolism ; Ribonucleoproteins/immunology/*physiology

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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Can we retrieve a clear paleoclimatic signal from the deeper part of the EPICA Dome C ice core? (2015)

Tison, J.-L. ; de Angelis, M. ; Littot, G. ; [et al.]

Copernicus Publications

In: EPIC3The Cryosphere Discussion, Copernicus Publications, 9, pp. 567-608, ISSN: 1994-0416

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Publication Date: 2015-02-10

Description: An important share of paleoclimatic information is buried within the lowermost layers of deep ice cores. Because improving our records further back in time is one of the main challenges in the near future, it is essential to judge how deep these records remain unaltered, since the proximity of the bedrock is likely to interfere both with the recorded temporal sequence and the ice properties. In this paper, we present a multiparametric study (δD-δ18Oice, δ18Oatm, total air content, CO2, CH4, N2O, dust, high resolution chemistry, ice texture) of the bottom 60m of the EPICA Dome C ice core from central Antarctica. These bottom layers have been subdivided in two sections: the lower 12m showing visible solid inclusions (basal ice) and the 48m above which we refer to as “deep ice”. Some of the data are consistent with a pristine paleoclimatic signal, others show clear anomalies. It is demonstrated that neither large scale bottom refreezing of subglacial water, nor mixing (be it internal or with a local basal end-term from a previous/ initial ice sheet configuration) can explain the observed bottom ice properties. We focus on the high-resolution chemical profiles and on the available remote sensing data on the subglacial topography of the site to propose a mechanism by which relative stretching of the bottom ice sheet layers is made possible, due to the progressively confining effect of subglacial valley sides. This stress field change, combined with bottom ice temperature close to the pressure melting point, induces accelerated migration recrystallization, which results in spatial chemical sorting of the impurities, depending on their state (dissolved vs. solid) and if they are involved or not in salt formation. This chemical sorting effect is responsible for the progressive build-up of the visible solid aggregates that therefore mainly originate “from within”, and not from incorporation processes of allochtone material at the ice–bedrock interface. We also discuss how the proposed mechanism is compatible with the other variables described. We conclude that the paleoclimatic signal is only marginally affected in terms of global ice properties at the bottom of EPICA Dome C, but that the time scale has been considerably distorted by mechanical stretching of MIS20 due to the increasing influence of the subglacial topography, a process that might have started well above the bottom ice.

Repository Name: EPIC Alfred Wegener Institut

Type: Article , notRev

Format: application/pdf

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