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. 1997 Oct;6(10):2268–2270. doi: 10.1002/pro.5560061023

Cloning, expression, and crystallization of a hyperthermophilic protein that is homologous to the eukaryotic translation initiation factor, eIF5A.

K K Kim 1, H Yokota 1, R Kim 1, S H Kim 1
PMCID: PMC2143566  PMID: 9336851

Abstract

A gene coding for a protein homologous to a translation initiation factor of eukaryotes, eIF5A, was cloned from Methanococcus jannaschii, a hyperthermophile with an optimum growth temperature of 85 degrees C. The protein was overexpressed, purified and crystallized. The crystals were obtained by vapor diffusion method with 8% PEG 4000 as precipitant and belong to space group P4(1)22 with unit cell dimensions a = b = 45.52 A and c = 155.59 A. These crystals diffract to at least 2.2 A resolution.

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Selected References

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  1. Cooper H. L., Park M. H., Folk J. E. Hypusine formation: a unique posttranslational modification in translation initiation factor eIF-4D. Methods Enzymol. 1984;106:344–351. doi: 10.1016/0076-6879(84)06034-1. [DOI] [PubMed] [Google Scholar]
  2. Hanauske-Abel H. M., Park M. H., Hanauske A. R., Popowicz A. M., Lalande M., Folk J. E. Inhibition of the G1-S transition of the cell cycle by inhibitors of deoxyhypusine hydroxylation. Biochim Biophys Acta. 1994 Mar 31;1221(2):115–124. doi: 10.1016/0167-4889(94)90003-5. [DOI] [PubMed] [Google Scholar]
  3. Kang H. A., Hershey J. W. Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae. J Biol Chem. 1994 Feb 11;269(6):3934–3940. [PubMed] [Google Scholar]
  4. Katahira J., Ishizaki T., Sakai H., Adachi A., Yamamoto K., Shida H. Effects of translation initiation factor eIF-5A on the functioning of human T-cell leukemia virus type I Rex and human immunodeficiency virus Rev inhibited trans dominantly by a Rex mutant deficient in RNA binding. J Virol. 1995 May;69(5):3125–3133. doi: 10.1128/jvi.69.5.3125-3133.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kemper W. M., Berry K. W., Merrick W. C. Purification and properties of rabbit reticulocyte protein synthesis initiation factors M2Balpha and M2Bbeta. J Biol Chem. 1976 Sep 25;251(18):5551–5557. [PubMed] [Google Scholar]
  6. Matthews B. W. Solvent content of protein crystals. J Mol Biol. 1968 Apr 28;33(2):491–497. doi: 10.1016/0022-2836(68)90205-2. [DOI] [PubMed] [Google Scholar]
  7. Ruhl M., Himmelspach M., Bahr G. M., Hammerschmid F., Jaksche H., Wolff B., Aschauer H., Farrington G. K., Probst H., Bevec D. Eukaryotic initiation factor 5A is a cellular target of the human immunodeficiency virus type 1 Rev activation domain mediating trans-activation. J Cell Biol. 1993 Dec;123(6 Pt 1):1309–1320. doi: 10.1083/jcb.123.6.1309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Schnier J., Schwelberger H. G., Smit-McBride Z., Kang H. A., Hershey J. W. Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol Cell Biol. 1991 Jun;11(6):3105–3114. doi: 10.1128/mcb.11.6.3105. [DOI] [PMC free article] [PubMed] [Google Scholar]

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