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Primary structure of elongation factor 2 around the site of ADP‐ribosylation is highly conserved from archaebacteria to eukaryotes

1985; Wiley; Volume: 185; Issue: 1 Linguagem: Inglês

10.1016/0014-5793(85)80736-5

1873-3468

Renate Gehrmann, Agnes Henschen, Friedrich Klink,

Streptococcal Infections and Treatments

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.