Structural Task Force

RNA polymerase complex

(Also known as: RNA-dependent RNA polymerase, RdRp complex, nsp12, nsp7, nsp8)

SARS-CoV-2 uses single-stranded RNA to encode its proteins, and hence belongs to a class of "single-stranded RNA viruses".

The virus requires a special protein to copy this rather large RNA genome, called an “RNA-dependent RNA polymerase”. This protein uses the viral RNA as a template to make a new copy of RNA, by stringing single ribonucleotides together like beads on a string.

RdRp (also called nsp12) enlists the help of several other proteins – nsp7, nsp8, nsp10, and nsp14.

Nsp7 and nsp8 work together to provide a ramp (called “sliding-poles”) for newly-made RNA to leave the polymerase smoothly. This may seem unnecessary, but the polymerase can’t make new RNA without it!

Nsp10 and nsp14 work together to proofread the newly-made RNA, cutting out any mistakes, which allows SARS-CoV-2 to have such a huge genome.

Together, these proteins form a complex machine that enables the virus to make many high-fidelity copies of itself.

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September 1, 2020
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Exoribonuclease is a domain of nsp14 responsible for chopping out nucleotides incorrectly added by RdRp. This enzyme allows the large 29.9 kb genome of SARS-CoV-2 and remains a worthwhile target for drugs to fight this virus.

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RNA Polymerase is central to virus replication, and Remdesivir stops it. How? Learn here!

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Coronavirus Structural Taskforce
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