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© Gail Rozen-Gagnon, Christine Schmitt,
Cells infected with Chikungunya (CHIK) virus.
Publication : Structure (London, England : 1993)

Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase VP1

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Structure (London, England : 1993) - 12 Nov 2008

Lu X, McDonald SM, Tortorici MA, Tao YJ, Vasquez-Del Carpio R, Nibert ML, Patton JT, Harrison SC

Link to Pubmed [PMID] – 19000820

Structure 2008 Nov;16(11):1678-88

Rotavirus RNA-dependent RNA polymerase VP1 catalyzes RNA synthesis within a subviral particle. This activity depends on core shell protein VP2. A conserved sequence at the 3′ end of plus-strand RNA templates is important for polymerase association and genome replication. We have determined the structure of VP1 at 2.9 A resolution, as apoenzyme and in complex with RNA. The cage-like enzyme is similar to reovirus lambda3, with four tunnels leading to or from a central, catalytic cavity. A distinguishing characteristic of VP1 is specific recognition, by conserved features of the template-entry channel, of four bases, UGUG, in the conserved 3′ sequence. Well-defined interactions with these bases position the RNA so that its 3′ end overshoots the initiating register, producing a stable but catalytically inactive complex. We propose that specific 3′ end recognition selects rotavirus RNA for packaging and that VP2 activates the autoinhibited VP1/RNA complex to coordinate packaging and genome replication.

https://www.ncbi.nlm.nih.gov/pubmed/19000820