Crystallization of a paraspeckle protein PSPC1-NONO heterodimer

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1231-4. doi: 10.1107/S1744309111026212. Epub 2011 Sep 29.

Abstract

The paraspeckle component 1 (PSPC1) and non-POU-domain-containing octamer-binding protein (NONO) heterodimer is an essential structural component of paraspeckles, ribonucleoprotein bodies found in the interchromatin space of mammalian cell nuclei. PSPC1 and NONO both belong to the Drosophila behaviour and human splicing (DBHS) protein family, which has been implicated in many aspects of RNA processing. A heterodimer of the core DBHS conserved region of PSPC1 and NONO comprising two tandemly arranged RNA-recognition motifs (RRMs), a NONA/paraspeckle (NOPS) domain and part of a predicted coiled-coil domain has been crystallized in space group C2, with unit-cell parameters a = 90.90, b = 67.18, c = 94.08 Å, β = 99.96°. The crystal contained one heterodimer in the asymmetric unit and diffracted to 1.9 Å resolution using synchrotron radiation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • DNA-Binding Proteins
  • Humans
  • Nuclear Matrix-Associated Proteins / chemistry*
  • Nuclear Matrix-Associated Proteins / metabolism
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism
  • Octamer Transcription Factors / chemistry*
  • Octamer Transcription Factors / metabolism
  • Protein Binding
  • Protein Multimerization*
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism

Substances

  • DNA-Binding Proteins
  • NONO protein, human
  • Nuclear Matrix-Associated Proteins
  • Nuclear Proteins
  • Octamer Transcription Factors
  • PSPC1 protein, human
  • RNA-Binding Proteins