HYP2 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome V.
Dietrich FS, Mulligan J, Hennessy K, Yelton MA, Allen E, Araujo R, Aviles E, Berno A, Brennan T, Carpenter J, Chen E, Cherry JM, Chung E, Duncan M, Guzman E, Hartzell G, Hunicke-Smith S, Hyman RW, Kayser A, Komp C, Lashkari D, Lew H, Lin D, Mosedale D, Davis RW
Nature387(6632 Suppl)78-81(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Data show that translation elongation factor eIF-5A (eIF5A) requirement for polyproline synthesis is imposed by proline, not by tRNAPro.
Title: Amino acid substrates impose polyamine, eIF5A, or hypusine requirement for peptide synthesis.

eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences.
Title: eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences.

eIF5A strongly promotes the translation of the stalling sequences identified by profiling and increases the rate of peptidyl-tRNA hydrolysis more than 17-fold.
Title: eIF5A Functions Globally in Translation Elongation and Termination.

the ability of eIF5A from tif51A-4 to bind to the ribosome while potentially blocking physical interaction with P-tRNA could explain its dominant negative phenotype.
Title: Mapping surface residues of eIF5A that are important for binding to the ribosome using alanine scanning mutagenesis.

tRNA. These findings would support a model whereby eIF-5A stimulates peptide bond formation on polyproline-stalled ribosomes by stabilizing and orienting the CCA-end of the P-tRNA
Title: Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome.