Primary structure of elongation factor 2 around the site of ADP‐ribosylation is highly conserved from archaebacteria to eukaryotes
- 3 June 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 185 (1) , 37-42
- https://doi.org/10.1016/0014-5793(85)80736-5
Abstract
Elongation factor 2 (EF‐2) from eukaryotes and archaebacteria can be ADP‐ribosylated by diphtheria toxin (DT) [(1977) Annu. Rev. Biochem. 46, 69‐94; (1980) Nature 287, 250‐251]. The primary structure of the ADP‐ribose accepting region in EFs from the archaebacteria Thermoplasma acidophilum, Halobacterium cutirubrum and Methanococcus vannielli was determined in order to elucidate the degree of conservation compared with 4 previously established eukaryotic sequences [(1971) FEBS Lett. 103, 253‐255]. Within a 9‐residue sequence including the site of ADP‐ribosylation 5 positions were found to be occupied by the same amino acid in all the archaebacterial and eukaryotic factors studied. There were more differences among the 3 archaebacterial sequences than among the 4 eukaryotic ones.Keywords
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