Specificities of Caenorhabditis elegans and human hairpin binding proteins for the first nucleotide in the histone mRNA hairpin loop

F Michel, D Schumperli, B Muller

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The 3' ends of animal replication-dependent histone mRNAs are formed by endonucleolytic cleavage of the primary transcripts downstream of a highly conserved RNA hairpin. The hairpin-binding protein (HBP) binds to this RNA element and is involved in histone RNA 3' processing. A minimal RNA-binding domain (RBD) of similar to 73 amino acids that has no similarity with other known RNA-binding motifs was identified in human HBP [Wang Z-F et al,, Genes & Dev, 1996, 10:3028-3040]. The primary sequence identity between human and Caenorhabditis elegans RBDs is 55% compared to 38% for the full-length proteins, We analyzed whether differences between C, elegans and human HBP and hairpins are reflected in the specificity of RNA binding. The C. elegans HBP and its RBB recognize only their cognate RNA hairpins, whereas the human HBP or RED can bind both the mammalian and the C. elegans hairpins. This selectivity of C, elegans HBP is mostly mediated by the first nucleotide in the loop, which is C in C. elegans and U in all other metazoans, By converting amino acids in the human RED to the corresponding C, elegans residues at places where the latter deviates from the consensus, we could identify two amino acid segments that contribute to selectivity for the first nucleotide of the hairpin loop.

Original languageEnglish
Pages (from-to)1539-1550
Number of pages12
JournalRNA
Volume6
Issue number11
Publication statusPublished - 2000

Keywords

  • RNA-binding domain
  • RNA-protein interaction
  • stem-loop-binding protein
  • pre-messenger-RNA
  • small nuclear nucleoprotein
  • 3' end formation
  • secondary structure
  • stem-loop
  • U7 SNRNP
  • 3'-end
  • sequences
  • invitro
  • recognition

Cite this