nsp13 helicase melts secondary structures in SARS-CoV-2 genomic RNA template

Stable Identifier
R-HSA-9694265
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
cytosol, double membrane vesicle viral factory outer membrane
ReviewStatus
5/5
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nsp13 helicase melts secondary structures in SARS-CoV-2 genomic RNA template
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nsp13 of SARS-CoV-2 possesses the nucleoside triphosphate hydrolase (NTPase) activity (Chen et al. 2020, Shu et al. 2020; Newman et al, 2021), and functions as an NTP-dependent RNA helicase that can unwind RNA helices (Shu et al. 2020; Mickolajczyk et al, 2021). Several G-quadruplex structures were confirmed in SARS-CoV-2 RNA and found to directly interact with nsp13, which may act to melt these structures (Ji et al. 2021).

nsp13 of SARS-CoV-1 is an ATP-dependent helicase that functions in the 5'-3' direction to unwind double stranded RNAs that have a 5' single strand overhang at least 20 nucleotides long. nsp13 can also act on double strand DNA in vitro, but dsRNA is thought to be its physiological substrate. The catalytic activity of SARS-CoV-1 nsp13 is increased in the presence of nsp12, the viral RNA-dependent RNA polymerase. nsp13 is needed for the replication of SARS-CoV-1 and is thought to act by melting secondary structures in the genomic RNA template during replication, and also to be involved in unwinding of RNA duplexes during transcription of viral genes. nsp13 is a promising target for experimental anti-SARS-CoV-1 drugs (Tanner et al. 2003, Ivanov et al. 2004, Bernini et al. 2006, Chen et al. 2009, Lee et al. 2010, Adedeji et al. 2012).
Literature References
PubMed ID Title Journal Year
33340543 Force-dependent stimulation of RNA unwinding by SARS-CoV-2 nsp13 helicase

Mickolajczyk, KJ, Shelton, PMM, Grasso, M, Cao, X, Warrington, SE, Aher, A, Liu, S, Kapoor, TM

Biophys J 2021
32484220 Discovery of G-quadruplex-forming sequences in SARS-CoV-2

Ji, D, Juhas, M, Tsang, CM, Kwok, CK, Li, Y, Zhang, Y

Brief. Bioinformatics 2020
32500504 SARS-Coronavirus-2 Nsp13 Possesses NTPase and RNA Helicase Activities That Can Be Inhibited by Bismuth Salts

Shu, T, Huang, M, Wu, D, Ren, Y, Zhang, X, Han, Y, Mu, J, Wang, R, Qiu, Y, Zhang, DY, Zhou, X

Virol Sin 2020
32783916 Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex

Chen, J, Malone, B, Llewellyn, E, Grasso, M, Shelton, PMM, Olinares, PDB, Maruthi, K, Eng, ET, Vatandaslar, H, Chait, BT, Kapoor, TM, Darst, SA, Campbell, EA

Cell 2020
34381037 Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase

Newman, JA, Douangamath, A, Yadzani, S, Yosaatmadja, Y, Aimon, A, Brandão-Neto, J, Dunnett, L, Gorrie-Stone, T, Skyner, R, Fearon, D, Schapira, M, von Delft, F, Gileadi, O

Nat Commun 2021
Participants
Input
Output
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as an event of
Catalyst Activity

5'-3' RNA helicase activity of SARS coronavirus 2 gRNA with secondary structure:RTC [double membrane vesicle viral factory outer membrane]

Physical Entity
SARS coronavirus 2 gRNA with secondary structure:RTC [double membrane vesicle viral factory outer membrane] (Severe acute respiratory syndrome coronavirus 2)
Activity
5'-3' RNA helicase activity (GO:0032574)
Disease
Name Identifier Synonyms
COVID-19 DOID:0080600 2019 Novel Coronavirus (2019-nCoV), Wuhan seafood market pneumonia virus infection, 2019-nCoV infection, Wuhan coronavirus infection
Cross References
Mondo
Authored
Orlic-Milacic, M  (2020-08-12)
Senff-Ribeiro, A  (2020-08-12)
Reviewed
Acencio, ML  (2020-09-09)
Created
Cook, J  (2020-07-07)
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