Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization

Caroline M. Groft, Stephen K. Burley

Research output: Contribution to journalArticlepeer-review

108 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1273-1283
Number of pages11
JournalMolecular cell
Volume9
Issue number6
DOIs
StatePublished - 2002
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization'. Together they form a unique fingerprint.

Cite this