English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

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

Lazzaretti, D., Bandholz-Cajamarca, L., Emmerich, C., Schaaf, K., Basquin, C., Irion, U., et al. (2018). The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity. Life science alliance, 1(5): e201800187. doi:10.26508/lsa.201800187.

Item is

Files

show Files
hide Files
:
e201800187.full.pdf (Publisher version), 3MB
Name:
e201800187.full.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
© 2018 Crown copyright. The government of Australia, Canada, or the UK ("the Crown") owns the copyright interests of authors who are government employees. The Crown Copyright is not transferable. https://creativecommons.org/licenses/by/4.0/

Locators

show

Creators

show
hide
 Creators:
Lazzaretti, Daniela1, Author
Bandholz-Cajamarca, Lina1, Author
Emmerich, Christiane1, Author
Schaaf, Kristina1, Author
Basquin, Claire2, Author           
Irion, Uwe1, Author
Bono, Fulvia1, Author
Affiliations:
1external, ou_persistent22              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

Content

show
hide
Free keywords: -
 Abstract: During mRNA localization, RNA-binding proteins interact with specific structured mRNA localization motifs. Although several such motifs have been identified, we have limited structural information on how these interact with RNA-binding proteins. Staufen proteins bind structured mRNA motifs through dsRNA-binding domains (dsRBD) and are involved in mRNA localization in Drosophila and mammals. We solved the structure of two dsRBDs of human Staufen1 in complex with a physiological dsRNA sequence. We identified interactions between the dsRBDs and the RNA sugar-phosphate backbone and direct contacts of conserved Staufen residues to RNA bases. Mutating residues mediating nonspecific backbone interactions only affected Staufen function in Drosophila when in vitro binding was severely reduced. Conversely, residues involved in base-directed interactions were required in vivo even when they minimally affected in vitro binding. Our work revealed that Staufen can read sequence features in the minor groove of dsRNA and suggests that these influence target selection in vivo.

Details

show
hide
Language(s): eng - English
 Dates: 2018-10-182018
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 30456389
DOI: 10.26508/lsa.201800187
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Life science alliance
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 1 (5) Sequence Number: e201800187 Start / End Page: - Identifier: ISSN: 2575-1077