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  • 1
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    Essential role for the SMN complex in the specificity of snRNP assembly (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-12-03
    Beschreibung: 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〉
    Schlagwort(e): 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
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation (2010)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2010-10-01
    Beschreibung: 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〉
    Schlagwort(e): 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
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
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    Heterogeneous nuclear ribonucleoproteins: role in RNA splicing (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1986-03-28
    Beschreibung: 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〉
    Schlagwort(e): 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
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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