NMR reveals specific tracts within the intrinsically disordered regions of the SARS-CoV-2 nucleocapsid protein involved in RNA encountering

  • The SARS-CoV-2 nucleocapsid (N) protein is crucial for the highly organized packaging and transcription of the genomic RNA. Studying atomic details of the role of its intrinsically disordered regions (IDRs) in RNA recognition is challenging due to the absence of structure and to the repetitive nature of their primary sequence. IDRs are known to act in concert with the folded domains of N and here we use NMR spectroscopy to identify the priming events of N interacting with a regulatory SARS-CoV-2 RNA element. 13C-detected NMR experiments, acquired simultaneously to 1H detected ones, provide information on the two IDRs flanking the N-terminal RNA binding domain (NTD) within the N-terminal region of the protein (NTR, 1–248). We identify specific tracts of the IDRs that most rapidly sense and engage with RNA, and thus provide an atom-resolved picture of the interplay between the folded and disordered regions of N during RNA interaction.

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Author:Letizia PontorieroORCiD, Marco SchiavinaORCiD, Sophie M. KornORCiDGND, Andreas SchlundtORCiDGND, Roberta PierattelliORCiD, Isabella C. FelliORCiD
URN:urn:nbn:de:hebis:30:3-721098
DOI:https://doi.org/10.3390/biom12070929
ISSN:2218-273X
Parent Title (English):Biomolecules
Publisher:MDPI
Place of publication:Basel
Document Type:Article
Language:English
Date of Publication (online):2022/07/02
Date of first Publication:2022/07/02
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2023/03/27
Tag:COVID-19; IDP; NMR; RNA; SARS-CoV-2
Volume:12
Issue:7
Page Number:13
First Page:1
Last Page:13
Note:
The following supporting information can be downloaded at: https://www.mdpi.com/article/10.3390/biom12070929/s1, Figure S1: molecular components used in this study [57,58]; Figure S2: Triplicates of EMSA gels. Figure S3: 2D HN spectra of NTR upon addiction of RNA; Figure S4: NetPhos results [59]; Figure S5: 3D-(H)CBCACON strips; Figure S6: CSP and PRE results. It also includes the additional references.
Note:
his work was funded in part by a grant from the Italian Ministry of University and Research (FISR2020IP_02112, ID-COVID), by Fondazione CR Firenze and with the support of the Italian government program “MIUR Dipartimenti di Eccellenza 2018–2022” (58503_DIPECC). This work was also supported by the Goethe Corona Funds, by the German Research Council (DFG) within CRC902 (“Molecular Principles of RNA-based regulation”) project part B18, through DFG grant number SCHL2062/2-1 to A.S., and by the Johanna Quandt Young Academy at Goethe through the financial support of A.S. (stipend number 2019/AS01).
HeBIS-PPN:508547024
Institutes:Biowissenschaften
Wissenschaftliche Zentren und koordinierte Programme / Zentrum für Biomolekulare Magnetische Resonanz (BMRZ)
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - CC BY - Namensnennung 4.0 International

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