Histone H3 N-terminal peptide binds directly to its own mRNA: a possible mode of feedback inhibition to control translation

Chembiochem. 2009 May 25;10(8):1313-6. doi: 10.1002/cbic.200900154.

Abstract

Give me some feedback: In vitro selection of aptamers against the H3 peptide provided specific hairpin RNAs that possess high homology with histone H3 mRNA. The identified H3 hairpin RNA binds specifically to the H3 peptide with micromolar affinity and dose-dependently inhibits in vitro translation of the H3 protein. Consequently, the hairpin RNA and H3 peptide are one of the rare cis- and trans-elements on coding regions found among housekeeping proteins in higher eukaryotes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aptamers, Nucleotide / metabolism
  • Base Sequence
  • Feedback, Physiological
  • Histones / genetics*
  • Histones / metabolism
  • Peptides / chemistry
  • Peptides / pharmacology*
  • Protein Biosynthesis*
  • RNA, Messenger / chemistry*
  • RNA, Messenger / metabolism

Substances

  • Aptamers, Nucleotide
  • Histones
  • Peptides
  • RNA, Messenger