A conserved charged single α-helix with a putative steric role in paraspeckle formation
- 1Pázmány Péter Catholic University, Faculty of Information Technology and Bionics, H-1083 Budapest, Hungary
- 2Eötvös Loránd University, Department of Biochemistry, H-1117 Budapest, Hungary
- Corresponding author: gaspari.zoltan{at}itk.ppke.hu
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.
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Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.053058.115.
- Received June 26, 2015.
- Accepted August 27, 2015.
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