Reactome | One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities

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One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities Show undefined attributes

author	[Person:9682260] Subissi, L [Person:9682262] Posthuma, CC [Person:9682265] Collet, A [Person:9682263] Zevenhoven-Dobbe, JC [Person:9614522] Gorbalenya, AE [Person:9682261] Decroly, E [Person:9681601] Snijder, EJ [Person:9681646] Canard, B [Person:9681654] Imbert, I
created	[InstanceEdit:9682264] Orlic-Milacic, Marija, 2020-04-08
dbId	9682259
displayName	One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities
journal	Proc. Natl. Acad. Sci. U.S.A.
pages	E3900-9
pubMedIdentifier	25197083
schemaClass	LiteratureReference
title	One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities
url	http://www.ncbi.nlm.nih.gov/pubmed/25197083
volume	111
year	2014

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[Summation:9694297] This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Non-structural protein 14 (nsp14) of the human SARS coronavirus is a bifunctional enzyme bearing 3'-5 exoribonuclease activity involved in replication fidelity and RNA cap N7-guanine methyltransferase activity involved in 5'-RNA capping. nsp14 binds to the minimal replication and transcription complex (RTC), composed of nsp7, nsp8, and nsp12, by directly binding to nsp12 (the main RNA-dependent RNA polymerase). Binding of nsp14 does not affect the processivity of the RTC (Minskaia et al. 2006, Subissi et al. 2014).
[Reaction:R-HSA-9682258] nsp14 binds nsp12
[Reaction:R-HSA-9682544] nsp14 binds nsp10
[Summation:9694704] The interaction between nsp10 and nsp14 is conserved in SARS...
[Summation:9694429] After synthesizing the complementary minus RNA of the plus s...
[Summation:9694486] This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The replication-transcription complex (RTC) completes synthesis of the genomic RNA complement (minus strand). The complex of nsp7 and nsp8 confers processivity to nsp12, the virally encoded RNA-dependent RNA polymerase that replicates the viral genomic RNA, enabling the RTC to complete the RNA synthesis with a very low dissociation rate. nsp7 plays a crucial role in maintaining binding of the RTC to the RNA. nsp14 subunit of the RTC does not affect the processivity (Subissi et al. 2014).
[Summation:9694744] Virally encoded RNA-dependent RNA polymerase (nsp12, also kn...
[BlackBoxEvent:R-HSA-9681840] RTC synthesizes SARS-CoV-1 plus strand genomic RNA
[BlackBoxEvent:R-HSA-9682465] RTC completes synthesis of the minus strand genomic RNA complement
[Reaction:R-HSA-9682603] nsp14 acts as a 3'-to-5' exonuclease to remove misincorporated nucleotides from nascent RNA
[BlackBoxEvent:R-HSA-9681674] nsp12 synthesizes minus strand SARS-CoV-1 genomic RNA complement
[Summation:9694564] In human SARS coronavirus 2 (SARS-CoV-2) nsp14 is essential ...

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