Back to Search
Start Over
Structural domains of SARS-CoV-2 nucleocapsid protein coordinate to compact long nucleic acid substrates.
- Source :
-
Nucleic acids research [Nucleic Acids Res] 2023 Jan 11; Vol. 51 (1), pp. 290-303. - Publication Year :
- 2023
-
Abstract
- The SARS-CoV-2 nucleocapsid (N) protein performs several functions including binding, compacting, and packaging the ∼30 kb viral genome into the viral particle. N protein consists of two ordered domains, with the N terminal domain (NTD) primarily associated with RNA binding and the C terminal domain (CTD) primarily associated with dimerization/oligomerization, and three intrinsically disordered regions, an N-arm, a C-tail, and a linker that connects the NTD and CTD. We utilize an optical tweezers system to isolate a long single-stranded nucleic acid substrate to measure directly the binding and packaging function of N protein at a single molecule level in real time. We find that N protein binds the nucleic acid substrate with high affinity before oligomerizing and forming a highly compact structure. By comparing the activities of truncated protein variants missing the NTD, CTD, and/or linker, we attribute specific steps in this process to the structural domains of N protein, with the NTD driving initial binding to the substrate and ensuring high localized protein density that triggers interprotein interactions mediated by the CTD, which forms a compact and stable protein-nucleic acid complex suitable for packaging into the virion.<br /> (© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Details
- Language :
- English
- ISSN :
- 1362-4962
- Volume :
- 51
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Nucleic acids research
- Publication Type :
- Academic Journal
- Accession number :
- 36533523
- Full Text :
- https://doi.org/10.1093/nar/gkac1179