The U7 snRNP and the hairpin binding protein: Key players in histone mRNA metabolism

Berndt Marino Muller, D Schumperli

Research output: Contribution to journalLiterature review

45 Citations (Scopus)

Abstract

Animal replication-de pendent histone mRNAs are subject to several post-transcriptional regulatory processes. Their nonpolyadenylated 3' ends are formed preferentially during S phase by a unique nuclear cleavage event. This requires the base pairing between U7 snRNA and a histone spacer element 3' of the cleavage site. Cleavage occurs preferentially after adenosine, at a fixed distance from the hybrid region. A conserved RNA hairpin just upstream of the cleavage site is recognised by the hairpin binding protein (HBP) that acts as an auxiliary processing factor, stabilising the interaction of the histone pre-mRNA with the U7 snRNP. The interaction between HBP and the RNA hairpin is very stable and HBP is also found associated with histone mRNAs on polysomes. The hairpin and presumably, HBP are also required for nuclear export and translation of histone mRNA. Furthermore, histone mRNAs are selectively destabilised in the G2 phase or upon inhibition of DNA synthesis and this regulation is also associated with the hairpin. Recently, HBP-encoding cDNAs were isolated from various organisms. Human, mouse and Xenopus laevis HBPs are similar, while the Caenorhabditis elegans protein has significant homology to the others only in a central RNA binding domain. (C) 1997 Academic Press Ltd.

Original languageEnglish
Pages (from-to)567-576
Number of pages10
JournalSeminars in Cell & Developmental Biology
Volume8
Issue number6
DOIs
Publication statusPublished - Dec 1997

Keywords

  • histone
  • RNA 3 ' processing
  • U7 small nuclear ribonucleoprotein
  • hairpin binding protein
  • stem-loop binding protein
  • RNA-protein interaction
  • SMALL NUCLEAR-RNA
  • PRE-MESSENGER-RNA
  • 3' END FORMATION
  • CELL CYCLE MUTANT
  • STEM-LOOP
  • PROCESSING REACTION
  • FLANKING SEQUENCES
  • GENE-TRANSCRIPTION
  • XENOPUS OOCYTES
  • SITE
  • RNA 3' processing
  • U& small nuclear ribonucleoprotein
  • stem-lopp binding protein

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