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Hexameric molecular motors: P4 packaging ATPase unravels the mechanism

journal contribution
posted on 2023-06-08, 19:50 authored by D E Kainov, R Tuma, Erika ManciniErika Mancini
Genome packaging into an empty capsid is an essential step in the assembly of many complex viruses. In double-stranded RNA (dsRNA) bacteriophages of the Cystoviridae family this step is performed by a hexameric helicase P4 which is one of the simplest packaging motors found in nature. Biochemical and structural studies of P4 proteins have led to a surprising finding that these proteins bear mechanistic and structural similarities to a variety of the pervasive RecA/F1-ATPase-like motors that are involved in diverse biological functions. This review describes the role of P4 proteins in assembly, transcription and replication of dsRNA bacteriophages as it has emerged over the past decade while focusing on the most recent structural studies. The P4 mechanism is compared with the models proposed for the related hexameric motors. © Birkhäuser Verlag, 2006.

History

Publication status

  • Published

Journal

Cellular and Molecular Life Sciences

ISSN

1420-682X

Publisher

Springer Verlag

Issue

10

Volume

63

Page range

1095-1105

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2015-01-29

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