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  • 1
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    Target RNA-directed trimming and tailing of small silencing RNAs (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-06-19
    Description: In Drosophila, microRNAs (miRNAs) typically guide Argonaute1 to repress messenger RNA (mRNA), whereas small interfering RNAs (siRNAs) guide Argonaute2 to destroy viral and transposon RNA. Unlike siRNAs, miRNAs rarely form extensive numbers of base pairs to the mRNAs they regulate. We find that extensive complementarity between a target RNA and an Argonaute1-bound miRNA triggers miRNA tailing and 3'-to-5' trimming. In flies, Argonaute2-bound small RNAs--but not those bound to Argonaute1--bear a 2'-O-methyl group at their 3' ends. This modification blocks target-directed small RNA remodeling: In flies lacking Hen1, the enzyme that adds the 2'-O-methyl group, Argonaute2-associated siRNAs are tailed and trimmed. Target complementarity also affects small RNA stability in human cells. These results provide an explanation for the partial complementarity between animal miRNAs and their targets.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2902985/" 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/PMC2902985/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ameres, Stefan L -- Horwich, Michael D -- Hung, Jui-Hung -- Xu, Jia -- Ghildiyal, Megha -- Weng, Zhiping -- Zamore, Phillip D -- F30AG030283/AG/NIA NIH HHS/ -- GM62862/GM/NIGMS NIH HHS/ -- GM65236/GM/NIGMS NIH HHS/ -- J 2832/Austrian Science Fund FWF/Austria -- R01 GM065236/GM/NIGMS NIH HHS/ -- R01 GM065236-08/GM/NIGMS NIH HHS/ -- R37 GM062862/GM/NIGMS NIH HHS/ -- R37 GM062862-10/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Jun 18;328(5985):1534-9. doi: 10.1126/science.1187058.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20558712" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Argonaute Proteins ; *Base Pairing ; Cell Line ; Drosophila Proteins/genetics/metabolism ; Drosophila melanogaster/embryology/genetics ; Eukaryotic Initiation Factors/metabolism ; Green Fluorescent Proteins/genetics ; Humans ; Methylation ; Methyltransferases/genetics/metabolism ; MicroRNAs/chemistry/genetics/*metabolism ; Models, Biological ; RNA Caps ; *RNA Stability ; RNA, Complementary ; RNA, Messenger/chemistry/genetics/*metabolism ; RNA, Small Interfering/chemistry/genetics/*metabolism ; RNA-Induced Silencing Complex/metabolism
    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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  • 2
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    Endogenous siRNAs derived from transposons and mRNAs in Drosophila somatic cells (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-04-12
    Description: Small interfering RNAs (siRNAs) direct RNA interference (RNAi) in eukaryotes. In flies, somatic cells produce siRNAs from exogenous double-stranded RNA (dsRNA) as a defense against viral infection. We identified endogenous siRNAs (endo-siRNAs), 21 nucleotides in length, that correspond to transposons and heterochromatic sequences in the somatic cells of Drosophila melanogaster. We also detected endo-siRNAs complementary to messenger RNAs (mRNAs); these siRNAs disproportionately mapped to the complementary regions of overlapping mRNAs predicted to form double-stranded RNA in vivo. Normal accumulation of somatic endo-siRNAs requires the siRNA-generating ribonuclease Dicer-2 and the RNAi effector protein Argonaute2 (Ago2). We propose that endo-siRNAs generated by the fly RNAi pathway silence selfish genetic elements in the soma, much as Piwi-interacting RNAs do in the germ line.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2953241/" 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/PMC2953241/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghildiyal, Megha -- Seitz, Herve -- Horwich, Michael D -- Li, Chengjian -- Du, Tingting -- Lee, Soohyun -- Xu, Jia -- Kittler, Ellen L W -- Zapp, Maria L -- Weng, Zhiping -- Zamore, Phillip D -- F30 AG030283-02/AG/NIA NIH HHS/ -- F30 AG030283-03/AG/NIA NIH HHS/ -- F30 AG030283-04/AG/NIA NIH HHS/ -- F30AG030283/AG/NIA NIH HHS/ -- GM080625/GM/NIGMS NIH HHS/ -- GM62862/GM/NIGMS NIH HHS/ -- GM65236/GM/NIGMS NIH HHS/ -- HG003367/HG/NHGRI NIH HHS/ -- P30 AI042845/AI/NIAID NIH HHS/ -- P30 AI042845-119008/AI/NIAID NIH HHS/ -- R01 AI043208/AI/NIAID NIH HHS/ -- R01 AI043208-08/AI/NIAID NIH HHS/ -- R01 GM062862/GM/NIGMS NIH HHS/ -- R01 GM062862-08/GM/NIGMS NIH HHS/ -- R01 GM062862-09/GM/NIGMS NIH HHS/ -- R01 GM065236/GM/NIGMS NIH HHS/ -- R01 GM065236-07/GM/NIGMS NIH HHS/ -- R01 GM065236-08/GM/NIGMS NIH HHS/ -- R01 GM080625/GM/NIGMS NIH HHS/ -- R01 GM080625-02/GM/NIGMS NIH HHS/ -- R01 GM080625-03/GM/NIGMS NIH HHS/ -- R01 HG003367/HG/NHGRI NIH HHS/ -- R01 HG003367-03/HG/NHGRI NIH HHS/ -- R37 GM062862/GM/NIGMS NIH HHS/ -- R37 GM062862-11/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 May 23;320(5879):1077-81. doi: 10.1126/science.1157396. Epub 2008 Apr 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18403677" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Argonaute Proteins ; Base Sequence ; Cell Line ; *DNA Transposable Elements ; Drosophila Proteins/genetics/metabolism ; Drosophila melanogaster/*genetics/metabolism ; Mutation ; RNA Helicases/genetics/metabolism ; *RNA Interference ; RNA, Double-Stranded/metabolism ; RNA, Messenger/*genetics ; RNA, Small Interfering/*genetics/*metabolism ; RNA-Induced Silencing Complex/genetics/metabolism ; Retroelements ; Ribonuclease III
    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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  • 3
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    Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-08
    Description: Most mitochondrial proteins are encoded in the nucleus and are translated on free cytoplasmic ribosomes as larger precursors containing amino-terminal "leader" sequences, which are removed after the precursors are taken up by mitochondria. We have deduced the complete primary structure of the precursor of a human mitochondrial matrix enzyme, ornithine transcarbamylase (OTC), from the nucleotide sequence of cloned complementary DNA. The amino-terminal leader peptide of OTC is 32 amino acids in length and contains four arginines but no acidic residues. Cleavage of the leader peptide from the "mature" protein occurs between glutamine and asparagine residues. The sequence of mature human OTC resembles that of the subunits of both OTC and aspartate transcarbamylase from Escherichia coli. The biological activity of the cloned OTC complementary DNA was tested by joining it with SV40 (an animal virus) regulatory elements and transfecting cultured HeLa cells, which do not normally express OTC. Both the precursor and mature forms of the OTC subunit were identified; in stable transformants, enzymatic activity was also detected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horwich, A L -- Fenton, W A -- Williams, K R -- Kalousek, F -- Kraus, J P -- Doolittle, R F -- Konigsberg, W -- Rosenberg, L E -- AM 09527/AM/NIADDK NIH HHS/ -- AM 12579/AM/NIADDK NIH HHS/ -- GM 31539/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Jun 8;224(4653):1068-74.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6372096" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; DNA, Mitochondrial/*genetics ; DNA, Recombinant/metabolism ; Escherichia coli/enzymology ; HeLa Cells/metabolism ; Humans ; Mitochondria/enzymology ; Ornithine Carbamoyltransferase/*genetics ; Protein Biosynthesis ; Rats
    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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  • 4
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    Human ornithine transcarbamylase locus mapped to band Xp21.1 near the Duchenne muscular dystrophy locus (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-09
    Description: The gene for the mitochondrial enzyme ornithine transcarbamylase was mapped to the short arm of the X chromosome by in situ hybridization experiments, with DNA complementary to the human ornithine transcarbamylase gene used as a probe. A series of cell lines with X chromosome abnormalities was used to localize the gene to band Xp21.1. Because the gene maps near the Duchenne muscular dystrophy locus, the ornithine transcarbamylase probe may be useful in carrier detection and prenatal diagnosis of Duchenne muscular dystrophy as well as of ornithine transcarbamylase deficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lindgren, V -- de Martinville, B -- Horwich, A L -- Rosenberg, L E -- Francke, U -- GM 32156/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 9;226(4675):698-700.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494904" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Chromosome Mapping ; DNA/metabolism ; Female ; Humans ; Male ; Mice ; Muscular Dystrophies/enzymology/*genetics ; Nucleic Acid Hybridization ; Ornithine Carbamoyltransferase/*genetics ; Prenatal Diagnosis ; Sex Chromosome Aberrations/genetics ; *X Chromosome
    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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