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  • 1
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    Delineation of mRNA export pathways by the use of cell-permeable peptides (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: The transport of messenger RNAs (mRNAs) from the nucleus to the cytoplasm involves adapter proteins that bind the mRNA as well as receptor proteins that interact with the nuclear pore complex. We demonstrate the utility of cell-permeable peptides designed to interfere with interactions between potential adapter and receptor proteins to define the pathways accessed by particular mRNAs. We show that HuR, a protein implicated in the stabilization of short-lived mRNAs containing AU-rich elements (AREs), serves as an adapter for c-fos mRNA export through two pathways. One involves the HuR shuttling domain, HNS, which exhibits a heat shock-sensitive interaction with transportin 2 (Trn2); the other involves two protein ligands of HuR-pp32 and APRIL-which contain leucine-rich nuclear export signals (NES) recognized by the export receptor CRM1. Heterokaryon and in situ hybridization experiments reveal that the peptides selectively block the nucleocytoplasmic shuttling of their respective adapter proteins without perturbing the overall cellular distribution of polyadenylated mRNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallouzi, I E -- Steitz, J A -- CA16038/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1895-901.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729309" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antennapedia Homeodomain Protein ; *Antigens, Surface ; Biological Transport/drug effects ; Cell Line ; *Cell Membrane Permeability ; Cell Nucleus/drug effects/*metabolism ; Cytoplasm/drug effects/*metabolism ; ELAV Proteins ; ELAV-Like Protein 1 ; Genes, fos/*genetics ; Heat-Shock Response ; Homeodomain Proteins/chemistry/metabolism ; Humans ; Karyopherins/metabolism ; Molecular Sequence Data ; Neuropeptides/chemistry/metabolism ; Nuclear Proteins/chemistry/metabolism ; Peptide Fragments/*metabolism/pharmacology ; Phosphoproteins/metabolism ; Protein Binding/drug effects ; Protein Structure, Tertiary ; RNA Stability ; RNA, Messenger/genetics/*metabolism ; RNA-Binding Proteins/antagonists & inhibitors/chemistry/*metabolism ; *Receptors, Cytoplasmic and Nuclear ; Regulatory Sequences, Nucleic Acid/genetics ; Reproducibility of Results ; Tetrahydrofolate Dehydrogenase/genetics ; *Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1 (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-08
    Description: In mammalian cells, splice junctions play a dual role in mRNA quality control: They mediate selective nuclear export of mature mRNA and they serve as a mark for mRNA surveillance, which subjects aberrant mRNAs with premature termination codons to nonsense-mediated decay (NMD). Here, we demonstrate that the protein RNPS1, a component of the postsplicing complex that is deposited 5' to exon-exon junctions, interacts with the evolutionarily conserved human Upf complex, a central component of NMD. Significantly, RNPS1 triggers NMD when tethered to the 3' untranslated region of beta-globin mRNA, demonstrating its role as a subunit of the postsplicing complex directly involved in mRNA surveillance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lykke-Andersen, J -- Shu, M D -- Steitz, J A -- CA 16038/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1836-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Molecular Biochemistry and Biophysics, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546874" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions/genetics/metabolism ; Animals ; Cell Line ; DNA-Binding Proteins/genetics/*metabolism ; Exons/*genetics ; Fungal Proteins/metabolism ; Globins/genetics ; HeLa Cells ; Humans ; Macromolecular Substances ; Mice ; Models, Biological ; Precipitin Tests ; Protein Binding ; RNA Helicases/metabolism ; RNA Splicing ; RNA, Messenger/genetics/*metabolism ; RNA-Binding Proteins/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Ribonucleoproteins ; Saccharomyces cerevisiae Proteins ; Trans-Activators ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Splicing takes a holliday (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steitz, J A -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):888-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06536-0812.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1386941" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Mammals ; Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Precursors/*genetics ; *RNA Splicing ; RNA, Small Nuclear/*genetics ; Ribonucleoproteins/*genetics ; Ribonucleoproteins, Small Nuclear ; Vertebrates
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Interactions of small nuclear RNA's with precursor messenger RNA during in vitro splicing (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-25
    Description: Precursor messenger RNA splicing requires multiple factors including U1, U2, U4, U5, and U6 small nuclear RNA's. The crosslinking reagent psoralen was used to analyze the interactions of these RNA's with an adenovirus precursor messenger RNA in HeLa nuclear extract. An endogenous U2-U4-U6 crosslinkable complex dissociated upon incubation with precursor messenger RNA. During splicing, U1, U2, U5, and U6 became crosslinked to precursor messenger RNA and U2, U5, and U6 became crosslinked to excised lariat intron. U2 also formed a doubly crosslinked complex with U6 and precursor messenger RNA. The U1, U5, and U6 crosslinks to the precursor messenger RNA mapped to intron sequences near the 5' splice site, whereas the U2 crosslink mapped to the branch site. The kinetics of crosslink formation and disappearance delineates a temporal pathway for the action of small RNA's in the spliceosome. Potential base pairing interactions between conserved sequences in the small nuclear RNA's and precursor messenger RNA at the sites of crosslinking suggest that the 5' splice site is defined in several steps prior to the first cleavage event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wassarman, D A -- Steitz, J A -- GM26154/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 25;257(5078):1918-25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, Haven, CT 06536.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411506" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Base Sequence ; Cell Nucleus/metabolism ; Cross-Linking Reagents ; HeLa Cells ; Humans ; In Vitro Techniques ; Macromolecular Substances ; Molecular Sequence Data ; RNA Precursors/metabolism ; *RNA Splicing ; RNA, Messenger/*metabolism ; RNA, Small Nuclear/*metabolism ; Ribonucleoproteins, Small Nuclear/*metabolism/ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Switching from repression to activation: microRNAs can up-regulate translation (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-12-01
    Description: AU-rich elements (AREs) and microRNA target sites are conserved sequences in messenger RNA (mRNA) 3' untranslated regions (3'UTRs) that control gene expression posttranscriptionally. Upon cell cycle arrest, the ARE in tumor necrosis factor-alpha (TNFalpha) mRNA is transformed into a translation activation signal, recruiting Argonaute (AGO) and fragile X mental retardation-related protein 1 (FXR1), factors associated with micro-ribonucleoproteins (microRNPs). We show that human microRNA miR369-3 directs association of these proteins with the AREs to activate translation. Furthermore, we document that two well-studied microRNAs-Let-7 and the synthetic microRNA miRcxcr4-likewise induce translation up-regulation of target mRNAs on cell cycle arrest, yet they repress translation in proliferating cells. Thus, activation is a common function of microRNPs on cell cycle arrest. We propose that translation regulation by microRNPs oscillates between repression and activation during the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vasudevan, Shobha -- Tong, Yingchun -- Steitz, Joan A -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1931-4. Epub 2007 Nov 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048652" target="_blank"〉PubMed〈/a〉
    Keywords: *3' Untranslated Regions ; Argonaute Proteins ; Base Pairing ; Cell Cycle ; Cell Line ; Cell Proliferation ; Computational Biology ; Eukaryotic Initiation Factor-2/genetics/metabolism ; *Gene Expression Regulation ; HMGA2 Protein/genetics ; HeLa Cells ; Humans ; Interphase ; MicroRNAs/*metabolism ; *Protein Biosynthesis ; RNA, Messenger/genetics/metabolism ; RNA-Binding Proteins/genetics/metabolism ; Ribonucleoproteins/metabolism ; Transfection ; Tumor Necrosis Factor-alpha/biosynthesis/*genetics ; *Up-Regulation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Down-regulation of a host microRNA by a Herpesvirus saimiri noncoding RNA (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-06-19
    Description: T cells transformed by Herpesvirus saimiri express seven viral U-rich noncoding RNAs of unknown function called HSURs. We noted that conserved sequences in HSURs 1 and 2 constitute potential binding sites for three host-cell microRNAs (miRNAs). Coimmunoprecipitation experiments confirmed that HSURs 1 and 2 interact with the predicted miRNAs in virally transformed T cells. The abundance of one of these miRNAs, miR-27, is dramatically lowered in transformed cells, with consequent effects on the expression of miR-27 target genes. Transient knockdown and ectopic expression of HSUR 1 demonstrate that it directs degradation of mature miR-27 in a sequence-specific and binding-dependent manner. This viral strategy illustrates use of a ncRNA to manipulate host-cell gene expression via the miRNA pathway.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3075239/" 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/PMC3075239/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cazalla, Demian -- Yario, Therese -- Steitz, Joan A -- CA16038/CA/NCI NIH HHS/ -- P01 CA016038/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Jun 18;328(5985):1563-6. doi: 10.1126/science.1187197.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20558719" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Pairing ; Binding Sites ; Callithrix ; Cell Line, Transformed ; Cell Transformation, Viral ; Conserved Sequence ; *Down-Regulation ; Herpesvirus 2, Saimiriine/*genetics/metabolism ; Humans ; Jurkat Cells ; MicroRNAs/chemistry/genetics/*metabolism ; *RNA Stability ; RNA, Untranslated/chemistry/*metabolism ; RNA, Viral/chemistry/*metabolism ; T-Lymphocytes
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Poly(A) tail recognition by a viral RNA element through assembly of a triple helix (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-11-27
    Description: Kaposi's sarcoma-associated herpesvirus produces a highly abundant, nuclear noncoding RNA, polyadenylated nuclear (PAN) RNA, which contains an element that prevents its decay. The 79-nucleotide expression and nuclear retention element (ENE) was proposed to adopt a secondary structure like that of a box H/ACA small nucleolar RNA (snoRNA), with a U-rich internal loop that hybridizes to and protects the PAN RNA poly(A) tail. The crystal structure of a complex between the 40-nucleotide ENE core and oligo(A)(9) RNA at 2.5 angstrom resolution reveals that unlike snoRNAs, the U-rich loop of the ENE engages its target through formation of a major-groove triple helix. A-minor interactions extend the binding interface. Deadenylation assays confirm the functional importance of the triple helix. Thus, the ENE acts as an intramolecular RNA clamp, sequestering the PAN poly(A) tail and preventing the initiation of RNA decay.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3074936/" 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/PMC3074936/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitton-Fry, Rachel M -- DeGregorio, Suzanne J -- Wang, Jimin -- Steitz, Thomas A -- Steitz, Joan A -- CA16038/CA/NCI NIH HHS/ -- GM022778/GM/NIGMS NIH HHS/ -- P01 CA016038/CA/NCI NIH HHS/ -- P01 CA016038-38/CA/NCI NIH HHS/ -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 GM026154/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Nov 26;330(6008):1244-7. doi: 10.1126/science.1195858.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry (MB&B), Howard Hughes Medical Institute (HHMI), Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536-9812, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21109672" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Cell Nucleus/genetics/metabolism ; Crystallography, X-Ray ; Herpesvirus 8, Human/*genetics ; Mutation ; *Nucleic Acid Conformation ; Poly A/chemistry/*metabolism ; *RNA Stability ; RNA, Messenger/chemistry/genetics/metabolism ; RNA, Nuclear/*chemistry/metabolism ; RNA, Untranslated/*chemistry/genetics/metabolism ; RNA, Viral/*chemistry/genetics/metabolism ; *Regulatory Sequences, Ribonucleic Acid ; Riboswitch
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Requirement for intron-encoded U22 small nucleolar RNA in 18S ribosomal RNA maturation (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: The nucleoli of vertebrate cells contain a number of small RNAs that are generated by the processing of intron fragments of protein-coding gene transcripts. The host gene (UHG) for intro-encoded human U22 is unusual in that it specifies a polyadenylated but apparently noncoding RNA. Depletion of U22 from Xenopus oocytes by oligonucleotide-directed ribonuclease H targeting prevented the processing of 18S ribosomal RNA (rRNA) at both ends. The appearance of 18S rRNA was restored by injection of in vitro-synthesized U22 RNA. These results identify a cellular function for an intron-encoded small RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tycowski, K T -- Shu, M D -- Steitz, J A -- GM26154/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1558-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06536.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985025" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Northern ; Cell Nucleolus/*chemistry ; Humans ; *Introns ; Molecular Sequence Data ; Oligonucleotide Probes ; Oocytes/metabolism ; RNA Precursors/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Nuclear/chemistry/*genetics/*physiology ; RNA, Ribosomal, 18S/*metabolism ; RNA, Small Nuclear/chemistry/*genetics/*physiology ; Xenopus
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Small RNA chaperones for ribosome biogenesis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steitz, J A -- Tycowski, K T -- GM26154/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1626-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06536-0812, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502072" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Cell Nucleolus/*metabolism ; Introns ; Nucleic Acid Conformation ; RNA Precursors/*metabolism ; *RNA Processing, Post-Transcriptional ; RNA, Ribosomal/*biosynthesis/metabolism ; RNA, Small Nuclear/genetics/*metabolism ; Ribonucleoproteins, Small Nuclear/*metabolism ; Ribosomes/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Highly diverged U4 and U6 small nuclear RNAs required for splicing rare AT-AC introns (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-27
    Description: Removal of a rare class of metazoan precursor messenger RNA introns with AU-AC at their termini is catalyzed by a spliceosome that contains U11, U12, and U5 small nuclear ribonucleoproteins. Two previously unidentified, low-abundance human small nuclear RNAs (snRNAs), U4atac and U6atac, were characterized as associated with the AT-AC spliceosome and necessary for AT-AC intron splicing. The excision of AT-AC introns therefore requires four snRNAs not found in the major spliceosome. With the use of psoralen crosslinking, a U6atac interaction with U12 was identified that is similar to a U6-U2 helix believed to contribute to the spliceosomal active center. The conservation of only limited U6atac sequences in the neighborhood of this interaction and the potential of U6atac to base pair with the 5' splice site consensus for AT-AC introns provide support for current models of the core of the spliceosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tarn, W Y -- Steitz, J A -- GM26154/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 27;273(5283):1824-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, Howard Hughes Medical Institute, New Haven, CT 06536-0812, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8791582" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Conserved Sequence ; Cross-Linking Reagents ; Exons ; Furocoumarins ; HeLa Cells ; Humans ; *Introns ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Precursors/*metabolism ; *RNA Splicing ; RNA, Small Nuclear/chemistry/*metabolism ; Ribonucleoproteins, Small Nuclear/*metabolism ; Spliceosomes/chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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