nsp13 helicase melts secondary structures in SARS-CoV-1 genomic RNA template

Stable Identifier
R-HSA-9682695
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Human SARS coronavirus
Compartment
cytosol, double membrane vesicle viral factory outer membrane
ReviewStatus
5/5
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nsp13 helicase melts secondary structures in SARS-CoV-1 genomic RNA template
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nsp13 is an ATP-dependent human SARS coronavirus 1 (SARS-CoV-1) 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 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
16579970 Tertiary structure prediction of SARS coronavirus helicase

Bernini, A, Spiga, O, Venditti, V, Prischi, F, Bracci, L, Huang, J, Tanner, JA, Niccolai, N

Biochem. Biophys. Res. Commun. 2006
12917423 The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases

Tanner, JA, Watt, RM, Chai, YB, Lu, LY, Lin, MC, Peiris, JS, Poon, LL, Kung, HF, Huang, JD

J. Biol. Chem. 2003
15140959 Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase

Ivanov, KA, Thiel, V, Dobbe, JC, van der Meer, Y, Snijder, EJ, Ziebuhr, J

J. Virol. 2004
22615777 Mechanism of nucleic acid unwinding by SARS-CoV helicase

Adedeji, AO, Marchand, B, te Velthuis, AJ, Snijder, EJ, Weiss, S, Eoff, RL, Singh, K, Sarafianos, SG

PLoS ONE 2012
19224332 Interaction between SARS-CoV helicase and a multifunctional cellular protein (Ddx5) revealed by yeast and mammalian cell two-hybrid systems

Chen, JY, Chen, WN, Poon, KM, Zheng, BJ, Lin, X, Wang, YX, Wen, YM

Arch. Virol. 2009
20671029 Cooperative translocation enhances the unwinding of duplex DNA by SARS coronavirus helicase nsP13

Lee, NR, Kwon, HM, Park, K, Oh, S, Jeong, YJ, Kim, DE

Nucleic Acids Res. 2010
Participants
Input
Output
Participates
as an event of
Catalyst Activity

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

Physical Entity
SARS coronavirus gRNA with secondary structure:RTC [double membrane vesicle viral factory outer membrane] (Human SARS coronavirus)
Activity
5'-3' RNA helicase activity (GO:0032574)
Disease
Name Identifier Synonyms
severe acute respiratory syndrome DOID:2945 SARS-CoV infection, SARS
Cross References
Mondo
Authored
Orlic-Milacic, M  (2020-04-30)
Reviewed
Acencio, ML  (2020-05-27)
Mazein, A  (2020-05-27)
Created
Orlic-Milacic, M  (2020-04-13)
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