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The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity

View ORCID ProfileDaniela Lazzaretti, Lina Bandholz-Cajamarca, Christiane Emmerich, Kristina Schaaf, Claire Basquin, View ORCID ProfileUwe Irion, View ORCID ProfileFulvia Bono  Correspondence email
Daniela Lazzaretti
1Max Planck Institute for Developmental Biology, Tübingen, Germany
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Lina Bandholz-Cajamarca
1Max Planck Institute for Developmental Biology, Tübingen, Germany
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Christiane Emmerich
1Max Planck Institute for Developmental Biology, Tübingen, Germany
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Kristina Schaaf
1Max Planck Institute for Developmental Biology, Tübingen, Germany
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Claire Basquin
2Max Planck Institute of Biochemistry, Martinsried, Germany
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Uwe Irion
1Max Planck Institute for Developmental Biology, Tübingen, Germany
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Fulvia Bono
1Max Planck Institute for Developmental Biology, Tübingen, Germany
3Living Systems Institute, University of Exeter, Exeter, UK
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  • For correspondence: f.bono@exeter.ac.uk
Published 18 October 2018. DOI: 10.26508/lsa.201800187
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Structure of Staufen1 with ARF1 RNA
Daniela Lazzaretti, Lina Bandholz-Cajamarca, Christiane Emmerich, Kristina Schaaf, Claire Basquin, Uwe Irion, Fulvia Bono
Life Science Alliance Oct 2018, 1 (5) e201800187; DOI: 10.26508/lsa.201800187

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Structure of Staufen1 with ARF1 RNA
Daniela Lazzaretti, Lina Bandholz-Cajamarca, Christiane Emmerich, Kristina Schaaf, Claire Basquin, Uwe Irion, Fulvia Bono
Life Science Alliance Oct 2018, 1 (5) e201800187; DOI: 10.26508/lsa.201800187
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Volume 1, No. 5
October 2018
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  • 3'READS + RIP defines differential Staufen1 binding to alternative 3'UTR isoforms and reveals structures and sequence motifs influencing binding and polysome association
  • A multipronged approach to understanding the form and function of hStaufen protein
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