John W. B. Hershey

Christopher S. Fraser4
Sandro R. Valentini2
Danuza Rossi2
Paulo E. G. Boldrin2
Cleslei F. Zanelli2
4Christopher S. Fraser
2Sandro R. Valentini
2Danuza Rossi
2Paulo E. G. Boldrin
2Cleslei F. Zanelli
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The delivery of Met-tRNA(i) to the 40S ribosomal subunit is thought to occur by way of a ternary complex (TC) comprising eIF2, GTP and Met-tRNA(i). We have generated from purified human proteins a stable multifactor complex (MFC) comprising eIF1, eIF2, eIF3 and eIF5, similar to the MFC reported in yeast and plants. A human MFC free of the ribosome also is(More)
The gene for translation initiation factor IF1, infA, has been identified by using two synthetic oligonucleotides to screen a Charon 30 library of Escherichia coli DNA. A recombinant lambda phage, C1921, was purified from a plaque positive for both probes. A 2.8 kb BglII fragment and a 2.0 kb HindIII fragment isolated from C1921 were subcloned into the(More)
  • Danuza Rossi, Natalia M. Barbosa, Fabio C. Galvão, Paulo E. G. Boldrin, John W. B. Hershey, Cleslei F. Zanelli +2 others
  • 2016
eIF5A is the only protein known to contain the essential and unique amino acid residue hypusine. eIF5A functions in both translation initiation due to its stimulation of methionyl-puromycin synthesis and translation elongation, being highly required for peptide-bound formation of specific ribosome stalling sequences such as poly-proline. The functional(More)
  • Natália M. Barbosa, Paulo E. G. Boldrin, Danuza Rossi, Priscila A. Yamamoto, Tatiana F. Watanabe, Vitor H. Serrão +4 others
  • 2016
The translation elongation factor eIF5A is conserved through evolution and is necessary to rescue the ribosome during translation elongation of polyproline-containing proteins. Although the site of eIF5A binding to the ribosome is known, no systematic analysis has been performed so far to determine the important residues on the surface of eIF5A required for(More)
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