Molecular Cell
Volume 9, Issue 6, June 2002, Pages 1273-1283
Journal home page for Molecular Cell

Article
Recognition of eIF4G by Rotavirus NSP3 Reveals a Basis for mRNA Circularization

https://doi.org/10.1016/S1097-2765(02)00555-5Get rights and content
Under an Elsevier user license
open archive

Abstract

Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3′ consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely α-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure.

Cited by (0)

4

Present address: Structural GenomiX, Inc., 10505 Roselle Street, San Diego, California 92121.