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    A member of the polymerase beta nucleotidyltransferase superfamily is required for RNA interference in C. elegans

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    Authors
    Chen, Chun-Chieh G.
    Simard, Martin J.
    Tabara, Hiroaki
    Brownell, Daniel R.
    McCollough, Jennifer A.
    Mello, Craig C.
    UMass Chan Affiliations
    Program in Molecular Medicine
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2005-02-23
    Keywords
    Amino Acid Sequence; Animals; Base Sequence; Caenorhabditis elegans; Caenorhabditis elegans Proteins; DNA Primers; Fertility; Gene Components; *Models, Biological; Molecular Sequence Data; Nucleotidyltransferases; *RNA Interference; RNA, Small Interfering; Reverse Transcriptase Polymerase Chain Reaction; Sequence Alignment; Sequence Analysis, DNA
    Life Sciences
    Medicine and Health Sciences
    
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    http://dx.doi.org/10.1016/j.cub.2005.01.009
    Abstract
    RNA interference (RNAi) is an ancient, highly conserved mechanism in which small RNA molecules (siRNAs) guide the sequence-specific silencing of gene expression . Several silencing machinery protein components have been identified, including helicases, RNase-related proteins, double- and single-stranded RNA binding proteins, and RNA-dependent RNA polymerase-related proteins . Work on these factors has led to the revelation that RNAi mechanisms intersect with cellular pathways required for development and fertility . Despite rapid progress in understanding key steps in the RNAi pathway, it is clear that many factors required for both RNAi and related developmental mechanisms have not yet been identified. Here, we report the characterization of the C. elegans gene rde-3. Genetic analysis of presumptive null alleles indicates that rde-3 is required for siRNA accumulation and for efficient RNAi in all tissues, and it is essential for fertility and viability at high temperatures. RDE-3 contains conserved domains found in the polymerase beta nucleotidyltransferase superfamily, which includes conventional poly(A) polymerases, 2'-5' oligoadenylate synthetase (OAS), and yeast Trf4p . These findings implicate a new enzymatic modality in RNAi and suggest possible models for the role of RDE-3 in the RNAi mechanism.
    Source
    Curr Biol. 2005 Feb 22;15(4):378-83. Link to article on publisher's site
    DOI
    10.1016/j.cub.2005.01.009
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/33473
    PubMed ID
    15723801
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    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.cub.2005.01.009
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      The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative Calpha mRNA expressed specifically in spermatogenic cells

      San Agustin, Jovenal T.; Wilkerson, Curtis G.; Witman, George B. (2000-09-12)
      cAMP-dependent protein kinase has a central role in the control of mammalian sperm capacitation and motility. Previous protein biochemical studies indicated that the only cAMP-dependent protein kinase catalytic subunit (C) in ovine sperm is an unusual isoform, termed C(s), whose amino terminus differs from those of published C isoforms of other species. Isolation and sequencing of cDNA clones encoding ovine C(s) and Calpha1 (the predominant somatic isoform) now reveal that C(s) is the product of an alternative transcript of the Calpha gene. C(s) cDNA clones from murine and human testes also were isolated and sequenced, indicating that C(s) is of ancient origin and widespread in mammals. In the mouse, C(s) transcripts were detected only in testis and not in any other tissue examined, including ciliated tissues and ovaries. Finally, immunohistochemistry of the testis shows that C(s) first appears in pachytene spermatocytes. This is the first demonstration of a cell type-specific expression for any C isoform. The conservation of C(s) throughout mammalian evolution suggests that the unique structure of C(s) is important in the subunit's localization or function within the sperm.
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