Rapid nucleolytic degradation of the small cytoplasmic Y RNAs during apoptosis.

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  • Additional Information
    • Source:
      Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
      Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
    • Subject Terms:
      Apoptosis*; RNA/*metabolism; Anisomycin/pharmacology ; Autoantigens/metabolism ; Base Sequence ; Caspase Inhibitors ; Dactinomycin/pharmacology ; Enzyme Inhibitors/pharmacology ; Humans ; Jurkat Cells ; Molecular Sequence Data ; Nucleic Acid Conformation ; Proto-Oncogene Proteins c-bcl-2/metabolism ; RNA, Antisense/genetics ; RNA, Messenger/metabolism ; RNA, Small Cytoplasmic ; Ribonucleoproteins/metabolism ; Zinc/pharmacology ; SS-B Antigen
    • Abstract:
      We have investigated the fate of the RNA components of small ribonucleoprotein particles in apoptotic cells. We show that the cytoplasmic Ro ribonucleoprotein-associated Y RNAs are specifically and rapidly degraded during apoptosis via a caspase-dependent mechanism. This is the first study describing the selective degradation of a specific class of small structural RNA molecules in apoptotic cells. Cleavage and subsequent truncation of Y RNAs was observed upon exposure of cells to a variety of apoptotic stimuli and were found to be inhibited by Bcl-2, zinc, and several caspase inhibitors. These results indicate that apoptotic degradation of Y RNAs is dependent on caspase activation, which suggests that the nucleolytic activity responsible for hY RNA degradation is activated downstream of the caspase cascade. The Y RNA degradation products remain bound by the Ro60 protein and in part also by the La protein, the only two proteins known to be stably associated with intact Ro ribonucleoprotein particles. The size of the Y RNA degradation products is consistent with the protection from degradation of the most highly conserved region of the Y RNAs by the bound Ro60 and La proteins. Our results indicate that the rapid abrogation of the yet unknown function of Y RNAs might be an early step in the systemic deactivation of the dying cell.
    • Grant Information:
      AR42689 United States AR NIAMS NIH HHS; K08AI01521 United States AI NIAID NIH HHS
    • Accession Number:
      0 (Autoantigens)
      0 (Caspase Inhibitors)
      0 (Enzyme Inhibitors)
      0 (Proto-Oncogene Proteins c-bcl-2)
      0 (RNA, Antisense)
      0 (RNA, Messenger)
      0 (RNA, Small Cytoplasmic)
      0 (RO60 protein, human)
      0 (Ribonucleoproteins)
      0 (SS-A antigen)
      1CC1JFE158 (Dactinomycin)
      63231-63-0 (RNA)
      6C74YM2NGI (Anisomycin)
      J41CSQ7QDS (Zinc)
    • Publication Date:
      Date Created: 19990824 Date Completed: 19990930 Latest Revision: 20231213
    • Publication Date:
      20240829
    • Accession Number:
      10.1074/jbc.274.35.24799
    • Accession Number:
      10455152