The isolated N terminus of Ring1B is a well-folded, monomeric fragment with native-like structure

Ana Isabel Martínez-Gómez, Sandra Villegas, David Aguado-Llera, Julio Bacarizo, Ana Cámara-Artigas, Miguel Vidal, José L. Neira

Research output: Contribution to journalArticleResearchpeer-review

1 Citation (Scopus)

Abstract

The Polycomb group (PcG) proteins assemble into Polycomb repressive complexes (PRCs), PRC1 and PRC2, which act as general transcriptional repressors. PRC1 comprises a variety of biochemical entities endowed with histone H2A monoubiquitylation activity conferred by really interesting new gene (RING) finger E3 ubiquitin ligases Ring1A and Ring1B. All PRC1 complexes contain Ring1 proteins which are essential for Polycomb epigenetic regulation. We have been able to express the isolated N-terminal region of Ring1B, N-Ring1B, comprising the first 221 residues of the 334-residue-long Ring1B. This fragment contains the 41-residue-long RING finger motif, and flanking sequences that form an interacting platform for PcG and non-PcG proteins. We found that the N-Ring1B is a well-folded, monomeric fragment, with native-like structure which unfolds irreversibly. The protein is capable of binding to an ubiquitin-conjugase protein (with an 85% of sequence similarity to the Ring1B physiological partner) with moderate affinity. © The Author 2013.
Original languageEnglish
Pages (from-to)1-11
JournalProtein Engineering, Design and Selection
Volume27
DOIs
Publication statusPublished - 1 Jan 2014

Keywords

  • FTIR/NMR
  • binding
  • circular dichroism
  • fluorescence
  • protein folding
  • protein stability

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