nsp14 acts as a 3'-to-5' exonuclease to remove misincorporated nucleotides from nascent RNA

Stable Identifier
Reaction [transition]
Homo sapiens
Related Species
Human SARS coronavirus
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

nsp14 acts as 3'-5' exonuclease (Minskaia et al. 2006, Chen et al. 2007) that preferentially excises mismatched nucleotides from double stranded RNA (Minskaia et al. 2006, Bouvet et al. 2012). Binding to nsp10 increases the exonuclease activity of nsp14 (Bouvet et al. 2012, Subissi et al. 2014, Bouvet et al. 2014). nsp14 increases the fidelity of human SARS coronavirus 1 (SARS-CoV-1) replication by the nsp12 RNA-dependent RNA polymerase by 21-fold (Eckerle et al. 2010).

Literature References
PubMed ID Title Journal Year
17927896 Biochemical characterization of exoribonuclease encoded by SARS coronavirus

Hu, T, Guo, D, Jiang, M, Chen, P, Liu, Q, Chen, XS

J. Biochem. Mol. Biol. 2007
22635272 RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex

Canard, B, Gluais, L, Subissi, L, Decroly, E, Imbert, I, Bouvet, M

Proc. Natl. Acad. Sci. U.S.A. 2012
20463816 Infidelity of SARS-CoV Nsp14-exonuclease mutant virus replication is revealed by complete genome sequencing

Li, K, Becker, MM, Scherbakova, S, Lu, X, Denison, MR, Graham, RL, Eckerle, LD, Halpin, RA, Stockwell, TB, Venter, E, Spiro, DJ, Baric, RS

PLoS Pathog. 2010
16549795 Discovery of an RNA virus 3'->5' exoribonuclease that is critically involved in coronavirus RNA synthesis

Campanacci, V, Canard, B, Hertzig, T, Minskaia, E, Gorbalenya, AE, Ziebuhr, J, Cambillau, C

Proc. Natl. Acad. Sci. U.S.A. 2006
25074927 Coronavirus Nsp10, a critical co-factor for activation of multiple replicative enzymes

Drosten, C, Canard, B, Betzi, S, Guillemot, JC, L├ęcine, P, Snijder, EJ, Pfefferle, S, Lugari, A, Decroly, E, Imbert, I, Posthuma, CC, Bernard, S, Zevenhoven, JC, Bouvet, M, Morelli, X

J. Biol. Chem. 2014
25197083 One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities

Canard, B, Collet, A, Gorbalenya, AE, Subissi, L, Decroly, E, Imbert, I, Posthuma, CC, Zevenhoven-Dobbe, JC, Snijder, EJ

Proc. Natl. Acad. Sci. U.S.A. 2014
Catalyst Activity

3'-5'-exoribonuclease activity of SARS coronavirus gRNA:RTC:nascent RNA minus strand with mismatched nucleotide [double membrane vesicle viral factory outer membrane]

Name Identifier Synonyms
severe acute respiratory syndrome DOID:2945 SARS-CoV infection, SARS
Cite Us!