A conserved charged single α-helix with a putative steric role in paraspeckle formation

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Paraspeckles are subnuclear particles involved in the regulation of mRNA expression. They are formed by the association of DBHS family proteins and the NEAT1 long noncoding RNA. Here, we show that a recently identified structural motif, the charged single α-helix, is largely conserved in the DBHS family. Based on the available structural data and a previously suggested multimerization scheme of DBHS proteins, we built a structural model of a (PSPC1/NONO)n multimer that might have relevance in paraspeckle formation. Our model contains an extended coiled-coil region that is followed by and partially overlaps with the predicted charged single α-helix. We suggest that the charged single α-helix can act as an elastic ruler governing the exact positioning of the dimeric core structures relative to each other during paraspeckle assembly along the NEAT1 noncoding RNA.

Original languageEnglish
Pages (from-to)2023-2029
Number of pages7
JournalRNA
Volume21
Issue number12
DOIs
Publication statusPublished - Dec 2015

    Fingerprint

Keywords

  • Charged single α-helix
  • Coiled coil
  • Multimerization
  • Paraspeckle
  • Structural modeling

ASJC Scopus subject areas

  • Molecular Biology

Cite this