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Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras

Authors
  • Hollmann, Nele Merret1, 2
  • Jagtap, Pravin Kumar Ankush1
  • Masiewicz, Pawel1
  • Guitart, Tanit3
  • Simon, Bernd1
  • Provaznik, Jan4
  • Stein, Frank5
  • Haberkant, Per5
  • Sweetapple, Lara Jayne1
  • Villacorta, Laura4
  • Mooijman, Dylan6
  • Benes, Vladimir4
  • Savitski, Mikhail M.5, 7
  • Gebauer, Fátima3, 8
  • Hennig, Janosch1
  • 1 Structural and Computational Biology Unit, EMBL Heidelberg, Meyerhofstraße 1, 69117 Heidelberg, Germany
  • 2 Collaboration for Joint PhD Degree between EMBL and Heidelberg University, Faculty of Biosciences, Heidelberg, Germany
  • 3 Gene Regulation, Stem Cells and Cancer Programme, Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain
  • 4 Genomics Core Facility, EMBL Heidelberg, Meyerhofstraße 1, 69117 Heidelberg, Germany
  • 5 Proteomics Core Facility, EMBL Heidelberg, Meyerhofstraße 1, 69117 Heidelberg, Germany
  • 6 Developmental Biology Unit, EMBL Heidelberg, Meyerhofstraße 1, 69117 Heidelberg, Germany
  • 7 Genome Biology Unit, EMBL Heidelberg, Meyerhofstraße 1, 69117 Heidelberg, Germany
  • 8 Universitat Pompeu Fabra (UPF), 08003 Barcelona, Spain
Type
Published Article
Journal
Cell Reports
Publisher
Elsevier
Publication Date
Jul 21, 2020
Volume
32
Issue
3
Identifiers
DOI: 10.1016/j.celrep.2020.107930
PMID: 32697992
PMCID: PMC7383231
Source
PubMed Central
Keywords
License
Unknown

Abstract

Hollmann et al. show how non-RNA-binding domains within Drosophila Unr, an RNA-binding protein, contribute to its RNA target specificity. The selectivity is mediated by interdomain contacts to the RNA-binding cold-shock domains, which restrict the protein shape.

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