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Mechanism of RNA packaging motor

journal contribution
posted on 2023-06-08, 19:50 authored by Erika ManciniErika Mancini, Roman Tuma
P4 proteins are hexameric RNA packaging ATPases of dsRNA bacteriophages of the Cystoviridae family. P4 hexamers are integral part of the inner polymerase core and play several essential roles in the virus replication cycle. P4 proteins are structurally related to the hexameric helicases and translocases of superfamily 4 (SF4) and other RecA-like ATPases. Recombinant P4 proteins retain their 5' to 3' helicase and translocase activity in vitro and thus serve as a model system for studying the mechanism of action of hexameric ring helicases and RNA translocation. This review summarizes the different roles that P4 proteins play during virus assembly, genome packaging, and transcription. Structural and mechanistic details of P4 action are laid out to and subsequently compared with those of the related hexameric helicases and other packaging motors. © 2012 Springer Science+Business Media, LLC.

History

Publication status

  • Published

Journal

Advances in Experimental Medicine and Biology

ISSN

0065-2598

Publisher

Springer US

Volume

726

Page range

609-629

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2015-01-30

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