Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD

FEBS Lett. 2016 Jul;590(14):2221-31. doi: 10.1002/1873-3468.12256. Epub 2016 Jun 28.

Abstract

Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein composed of a small folded WW domain and a long disordered region. PQBP1 binds to spliceosomal proteins WBP11 and U5-15kD through its N-terminal WW domain and C-terminal region, respectively. Here, we reveal that the binding between PQBP1 and WBP11 reduces the binding affinity between PQBP1 and U5-15kD. Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism.

Keywords: allosteric mechanism; interaction; intrinsically disordered protein.

Publication types

  • Letter

MeSH terms

  • Allosteric Regulation / physiology
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Humans
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Protein Binding / physiology
  • Protein Domains
  • RNA Splicing Factors
  • Ribonucleoprotein, U5 Small Nuclear / chemistry*
  • Ribonucleoprotein, U5 Small Nuclear / genetics
  • Ribonucleoprotein, U5 Small Nuclear / metabolism

Substances

  • Carrier Proteins
  • DNA-Binding Proteins
  • Nuclear Proteins
  • PQBP1 protein, human
  • RNA Splicing Factors
  • Ribonucleoprotein, U5 Small Nuclear
  • TXNL4A protein, human
  • WBP11 protein, human