Viral small nuclear ribonucleoproteins bind a protein implicated in messenger RNA destabilization.

  • Myer V
  • Lee S
  • Steitz J
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Abstract

Herpesvirus saimiri (HVS) is one of several primate viruses that carry genes for small RNAs. The five H. saimiri-encoded U RNAs (HSURs) are the most abundant viral transcripts expressed in transformed marmoset T lymphocytes. They assemble with host proteins common to spliceosomal small nuclear ribonucleoproteins (snRNPs). HSURs 1, 2, and 5 exhibit sequences at their 5' ends identical to the AUUUA motif, which targets a number of protooncogene, cytokine, and lymphokine mRNAs for rapid degradation. We show that a 32-kDa protein previously demonstrated to bind to the 3' untranslated region of several unstable messages can be UV crosslinked specifically to HSUR 1, 2, and 5 transcripts in vitro, as well as to endogenous HSUR snRNPs. Our results suggest an unusual role for these viral snRNPs: HSURs may function to attenuate the rapid degradation of certain cellular mRNAs, thereby facilitating viral transformation of host T lymphocytes.

Author-supplied keywords

  • Base Sequence
  • Binding Sites
  • Cloning, Molecular
  • Herpesvirus 2, Saimiriine
  • Herpesvirus 2, Saimiriine: genetics
  • Molecular Sequence Data
  • Nuclear Proteins
  • Nuclear Proteins: metabolism
  • Protein Binding
  • RNA, Messenger
  • RNA, Messenger: metabolism
  • RNA, Viral
  • RNA, Viral: metabolism
  • Ribonucleoproteins
  • Ribonucleoproteins, Small Nuclear
  • Ribonucleoproteins: metabolism
  • Ribonucleoproteins: radiation effects
  • Ultraviolet Rays

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Authors

  • V E Myer

  • S I Lee

  • J a Steitz

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