Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent

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Gentz, Petra M, Blatch, Gregory L and Dorrington, Rosemary A (2009) Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent. FEBS Journal, 276 (3). pp. 695-706. ISSN 1742-464X (print) online (1742-4658)

Abstract

Post-translational modification of the highly conserved K51 residue of the Saccharomyces cerevisiae eukaryotic translation initiation factor 5A (eIF5A) to form hypusine, is essential for its many functions including the binding of specific mRNAs. We characterized hypusinated yeast eIF5A by size-exclusion chromatography and native PAGE, showing that the protein exists as a homodimer. A K51R mutant, which was not functional in vivo eluted as a monomer and inhibition of hypusination abolished dimerization. Furthermore, treatment of dimeric eIF5A with RNase A resulted in disruption of the dimer, leading us to conclude that RNA binding is also required for dimerization of eIF5A. We present a model of dimerization, based on the Neurospora crassa structural analogue, HEX-1.

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Item type Article
URI https://vuir.vu.edu.au/id/eprint/8144
DOI https://doi.org/10.1111/j.1742-4658.2008.06817.x
Official URL http://dx.doi.org/10.1111/j.1742-4658.2008.06817.x
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 0601 Biochemistry and Cell Biology
Keywords ResPubID22198. eIF5A, homodimer, hypusine, RNA binding, yeast
Citations in Scopus 14 - View on Scopus
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