Molecular, functional and structural properties of an archaebacterial elongation factor 2

Gennaro Raimo, Mariorosario Masullo, Augusto Parente, Antonio Dello Russo, Vincenzo Bocchini

Research output: Contribution to journalArticlepeer-review


The elongation factor 2 (aEF-2) from the extreme thermo-acidophilic archaebacterium Sulfolobus solfataricus, is the only cytosolic target protein which is ADP-ribosylated by diphtheria toxin in presence of NAD. Once ADP-ribosylated, aEF-2 is no longer able to sustain poly(Phe) synthesis in vitro. aEF-2 displays a great thermoresistance: at the growth temperature of the archaebacterium, 87°C, its half-life is 3 h. The amino acid sequence of the N-terminal region of aEF-2 has been determined up to residue 22. In the first 15 positions such a sequence is identical to that of EF-2 from Sulfolobus acidocaldarius and very similar to that of EF-2 from other archaebacteria or eukaryotes. The same is true for the primary structure of the peptide containing the ADP-ribosylation site. The fact that the primary structure of EF-2 at the ADP-ribosylation site is highly conserved ensures either the correct recognition of the histidine residue by the enzymes involved in its modification to diphthamide, or the proper interaction with the diphtheria toxin.

Original languageEnglish
Pages (from-to)127-132
Number of pages6
JournalBBA - Gene Structure and Expression
Issue number2
Publication statusPublished - Sep 24 1992


  • ADP-ribosylation
  • Elongation factor 2
  • Protein synthesis
  • Thermostability

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics
  • Structural Biology


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