title: Human rhinovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different.
abstract: Several picornaviruses shut down host cellular protein synthesis by proteolytic cleavage of the eukaryotic initiation factor (eIF) 4GI and eIF4GII isoforms. Viral RNA translation is maintained by a cap-independent mechanism. Here, we identify the human rhinovirus 2 2A(pro) cleavage site in eIF4GII in vitro as PLLNV(699)*GSR; this sequence lies seven amino acids C-terminal to the cleavage site previously identified in eIF4GI (LSTR681*GPP).
authors.affiliation: Department of Biochemistry and McGill Cancer Center, McGill University, Montreal, Quebec, Canada H3G 1Y6.
authors.forename: Alessandra
authors.initials: A
authors.lastname: Gradi
authors.forename: Yuri V
authors.initials: YV
authors.lastname: Svitkin
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Sommergruber
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Imataka
authors.forename: Shigenobu
authors.initials: S
authors.lastname: Morino
authors.forename: Tim
authors.initials: T
authors.lastname: Skern
authors.forename: Nahum
authors.initials: N
authors.lastname: Sonenberg
mesh_terms: D000595:Amino Acid Sequence; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D039603:Eukaryotic Initiation Factor-4G; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010448:Peptide Initiation Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012229:Rhinovirus / Q000201:enzymology*; D016415:Sequence Alignment; D014764:Viral Proteins
chemical_list: C113920:EIF4G1 protein, human; C491300:EIF4G2 protein, human; D039603:Eukaryotic Initiation Factor-4G; D010446:Peptide Fragments; D010448:Peptide Initiation Factors; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; C057400:picornain 2A, Picornavirus