Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68

Mikael Feracci, Jaelle N. Foot, Sushma N. Grellscheid, Marina Danilenko, Ralf Stehle, Oksana Gonchar, Hyun-Seo Kang, Caroline Dalgliesh, N. Helge Meyer, Yilei Liu, Albert Lahat, Michael Sattler, Ian C. Eperon, David J. Elliott and Cyril Dominguez ()
Additional contact information
Mikael Feracci: University of Leicester
Jaelle N. Foot: University of Leicester
Sushma N. Grellscheid: Institute of Genetic Medicine, Newcastle University, Central Parkway
Marina Danilenko: Institute of Genetic Medicine, Newcastle University, Central Parkway
Ralf Stehle: Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
Oksana Gonchar: University of Leicester
Hyun-Seo Kang: Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
Caroline Dalgliesh: Institute of Genetic Medicine, Newcastle University, Central Parkway
N. Helge Meyer: Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
Yilei Liu: Institute of Genetic Medicine, Newcastle University, Central Parkway
Albert Lahat: School of Biological and Biomedical Sciences, University of Durham
Michael Sattler: Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
Ian C. Eperon: University of Leicester
David J. Elliott: Institute of Genetic Medicine, Newcastle University, Central Parkway
Cyril Dominguez: University of Leicester

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract Sam68 and T-STAR are members of the STAR family of proteins that directly link signal transduction with post-transcriptional gene regulation. Sam68 controls the alternative splicing of many oncogenic proteins. T-STAR is a tissue-specific paralogue that regulates the alternative splicing of neuronal pre-mRNAs. STAR proteins differ from most splicing factors, in that they contain a single RNA-binding domain. Their specificity of RNA recognition is thought to arise from their property to homodimerize, but how dimerization influences their function remains unknown. Here, we establish at atomic resolution how T-STAR and Sam68 bind to RNA, revealing an unexpected mode of dimerization different from other members of the STAR family. We further demonstrate that this unique dimerization interface is crucial for their biological activity in splicing regulation, and suggest that the increased RNA affinity through dimer formation is a crucial parameter enabling these proteins to select their functional targets within the transcriptome.

Date: 2016
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms10355 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10355

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms10355

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().