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  • 1
    Publication Date: 1984-08-31
    Description: The splicing of messenger RNA precursors in vitro proceeds through an intermediate that has the 5' end of the intervening sequence joined to a site near the 3' splice site. This lariat structure, which has been characterized for an adenovirus 2 major late transcript, has a branch point, with 2'-5' and 3'-5' phosphodiester bonds emanating from a single adenosine residue. The excised intervening sequence retains the branch site and terminates in a guanosine residue with a 3' hydroxyl group. The phosphate group at the splice junction between the two exons originates from the 3' splice site at the precursor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Padgett, R A -- Konarska, M M -- Grabowski, P J -- Hardy, S F -- Sharp, P A -- P01-CA14051/CA/NCI NIH HHS/ -- P01-CA26717/CA/NCI NIH HHS/ -- R01-GM32467/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):898-903.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6206566" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/metabolism ; Base Sequence ; Chemical Phenomena ; Chemistry ; Nucleic Acid Conformation ; Nucleic Acid Precursors/analysis/*metabolism ; Oligoribonucleotides/metabolism ; Phosphates/metabolism ; RNA/analysis/*metabolism ; RNA Precursors ; *RNA Splicing ; RNA, Messenger/analysis/*metabolism ; RNA, Viral/analysis/*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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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-02-13
    Description: A general mechanism for the splicing of nuclear messenger RNA precursors in eukaryotic cells has been widely accepted. This mechanism, which generates lariat RNAs possessing a branch site, seems related to the RNA-catalyzed reactions of self-splicing introns. The splicing of nuclear messenger RNA precursors involves the formation of a multicomponent complex, the spliceosome. This splicing body contains at least three different small nuclear ribonucleoprotein particles (snRNPs), U2, U5, and U4 + U6. A complex containing precursor RNA and the U2 snRNP particle is a likely intermediate in the formation of the spliceosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharp, P A -- CA14051/CA/NCI NIH HHS/ -- GM34277/GM/NIGMS NIH HHS/ -- P01-CA42063/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):766-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3544217" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Introns ; Mutation ; Nucleic Acid Precursors/*genetics ; Protein Biosynthesis ; RNA Precursors ; *RNA Splicing ; RNA, Catalytic ; RNA, Messenger/*genetics ; RNA, Ribosomal/genetics ; RNA, Small Nuclear/genetics ; Saccharomyces cerevisiae/genetics ; Tetrahymena/genetics
    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
    Publication Date: 1986-09-19
    Description: The splicing process, which removes intervening sequences from messenger RNA (mRNA) precursors is essential to gene expression in eukaryotic cells. This site-specific process requires precise sequence recognition at the boundaries of an intervening sequence, but the mechanism of this recognition is not understood. The splicing of mRNA precursors occurs in a multicomponent complex termed the spliceosome. Such an assembly of components is likely to play a key role in specifying those sequences to be spliced. In order to analyze spliceosome structure, a stringent approach was developed to obtain splicing complexes free of cellular contaminants. This approach is a form of affinity chromatography based on the high specificity of the biotin-streptavidin interaction. A minimum of three subunits: U2, U5, and U4 + U6 small nuclear ribonucleoprotein particles were identified in the 35S spliceosome structure, which also contains the bipartite RNA intermediate of splicing. A 25S presplicing complex contained only the U2 particle. The multiple subunit structure of the spliceosome has implications for the regulation of a splicing event and for its possible catalysis by ribozyme or ribozymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grabowski, P J -- Sharp, P A -- CA 14051/CA/NCI NIH HHS/ -- GM32467/GM/NIGMS NIH HHS/ -- GM34277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 19;233(4770):1294-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3638792" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins ; Biotin ; Cell Nucleus/metabolism ; Chromatography, Affinity ; RNA Precursors ; *RNA Splicing ; RNA, Small Nuclear/*isolation & purification ; Ribonucleoproteins/*isolation & purification ; Streptavidin ; Xenopus
    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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