The Function of the Hypusine-containing Proteins of Yeast and Other Eukaryotes is Well Conserved

Overview

Journal Mol Gen Genet

Specialties Genetics
Molecular Biology

Date 1994 Sep 28

PMID 7969034

Citations 13

Authors

V Magdolen

H Klier

T WOHL

F Klink

H Hirt

J HAUBER

F Lottspeich

Affiliations

Soon will be listed here.

Abstract

The hypusine-containing protein (Hypp) is highly conserved in evolution, from man to archaebacteria, but is not found in eubacteria. Hypp is essential for the viability for yeast cells, where two forms are encoded by the genes HYP1 and HYP2. The hypusine-containing protein Hyp2p, encoded by the HYP2 gene in yeast, is present under both aerobic and anaerobic conditions, whereas Hyp1p synthesis is restricted to anaerobiosis. hyp1 disruption mutants grown under anaerobic conditions reveal no detectable alteration in phenotype relative to wild-type strains. We demonstrate that either Hyp1p or Hyp2p alone is sufficient for normal growth under both metabolic conditions. Moreover, Hypp from various eukaryotic species (slime mold, alfalfa and man) carries the lysine to hypusine modification when expressed in yeast and can substitute functionally for Hyp2p in strains disrupted for HYP2, indicating a highly conserved function of this protein. In contrast, the archaebacterial Hypp expressed in yeast is neither modified by hypusine, nor does it allow growth of cells deficient for yeast Hypp.

Citing Articles

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Suppression of Ribosomal Pausing by eIF5A Is Necessary to Maintain the Fidelity of Start Codon Selection.

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Amino acid substrates impose polyamine, eIF5A, or hypusine requirement for peptide synthesis.

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Posttranslational hypusination of the eukaryotic translation initiation factor-5A regulates Fusarium graminearum virulence.

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The hypusine-containing translation factor eIF5A.

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