Open AccessCrystallization of a paraspeckle protein PSPC1–NONO heterodimer
Author(s) -
Passon Daniel M.,
Lee Mihwa,
Fox Archa H.,
Bond Charles S.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111026212
Subject(s) - microbiology and biotechnology , rna splicing , rna , ribonucleoprotein , histone octamer , chemistry , rna binding protein , crystallography , biology , biophysics , histone , biochemistry , nucleosome , dna , gene
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 C 2, 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.