A genome-wide RNA interference screen reveals that variant histones are necessary for replication-dependent histone pre-mRNA processing

Mol Cell. 2007 Nov 30;28(4):692-9. doi: 10.1016/j.molcel.2007.10.009.

Abstract

Metazoan replication-dependent histone mRNAs are not polyadenylated and instead end in a conserved stem loop that is the cis element responsible for coordinate posttranscriptional regulation of these mRNAs. Using biochemical approaches, only a limited number of factors required for cleavage of histone pre-mRNA have been identified. We therefore performed a genome-wide RNA interference screen in Drosophila cells using a GFP reporter that is expressed only when histone pre-mRNA processing is disrupted. Four of the 24 genes identified encode proteins also necessary for cleavage/polyadenylation, indicating mechanistic conservation in formation of different mRNA 3' ends. We also unexpectedly identified the histone variants H2Av and H3.3A/B. In H2Av mutant cells, U7 snRNP remains active but fails to accumulate at the histone locus, suggesting there is a regulatory pathway that coordinates the production of variant and canonical histones that acts via localization of essential histone pre-mRNA processing factors.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Base Sequence
  • DNA Replication*
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / cytology
  • Genes, Reporter
  • Genome, Insect / genetics*
  • Histones / genetics
  • Histones / metabolism*
  • Molecular Sequence Data
  • Mutant Proteins / metabolism*
  • Polyadenylation
  • Protein Transport
  • RNA Interference*
  • RNA Precursors / genetics
  • RNA Precursors / metabolism*
  • RNA Processing, Post-Transcriptional*
  • Ribonucleoprotein, U7 Small Nuclear / metabolism

Substances

  • Drosophila Proteins
  • Histones
  • Mutant Proteins
  • RNA Precursors
  • Ribonucleoprotein, U7 Small Nuclear