PMID: 1907914Aug 1, 1991Paper

Properties of the elongation factor 1 alpha in the thermoacidophilic archaebacterium Sulfolobus solfataricus

European Journal of Biochemistry
Mariorosario MasulloV Bocchini

Abstract

The elongation factor 1 alpha (aEF-1 alpha) was purified to homogeneity from the thermoacidophilic archaebacterium Sulfolobus solfataricus by chromatographic procedures utilising DEAE-Sepharose, hydroxyapatite and FPLC on Mono S. The purified protein binds [3H]GDP at a 1:1 molar ratio and it is essential for poly(Phe) synthesis in vitro; it also binds GTP but not ATP. These findings indicate that aEF-1 alpha is the counterpart of the eubacterial elongation factor Tu (EF-Tu). Purified aEF-1 alpha is a monomeric protein with a relative molecular mass of 49,000 as determined by SDS/PAGE and by gel filtration on Sephadex G-100; its isoelectric point is 9.1. The overall amino acid composition did not reveal significant differences when compared with the amino acid composition of eubacterial EF-Tu from either Escherichia coli or Thermus thermophilus, of eukaryotic EF-1 alpha from Artemia salina or of archaebacterial EF-1 alpha from Methanococcus vannielii. The close similarities between the average hydrophobicity and the numbers of hydrogen-bond-forming or non-helix-forming residues suggest that common structural features exist among the factors compared. aEF-1 alpha shows remarkable thermophilic properties, as demonstrated by the ra...Continue Reading

References

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Citations

Aug 4, 2004·Extremophiles : Life Under Extreme Conditions·Mariorosario MasulloPaolo Arcari
Apr 18, 2008·Extremophiles : Life Under Extreme Conditions·Pasquale GrimaldiMariorosario Masullo
Apr 11, 1993·Nucleic Acids Research·P ArcariV Bocchini
Nov 8, 2007·Chemical Biology & Drug Design·Stefania StingoMaurizio Bifulco
Jan 19, 1995·Biochimica Et Biophysica Acta·M R Faraone-MennellaB Farina
Sep 24, 1992·Biochimica Et Biophysica Acta·G RaimoV Bocchini

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