Properties of the purified elongation factor 2 in the thermoacidophilic archaebacterium Sulfolobus solfataricus.
The elongation factor 2 (aEF-2) has been purified to homogeneity from the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus. It is the only target protein which is ADP-ribosylated by diphtheria toxin in presence of NAD and this modification abolishes its property to support poly(Phe) synthesis in vitro. The factor is constituted by a single polypeptide chain with a relative molecular mass of 78,000 and an isoelectric point of 5.9. aEF-2 is resistant to heat denaturation as shown by the fact that its capability to be ADP-ribosylated was only 10% reduced after 4 h treatment at 80 degrees C. Its amino acid composition does not reveal significant differences with that of analogous factors in other sources; nevertheless, the deviation function indicates that aEF-2 is related to Sulfolobus acidocaldarius and eukaryotes EF-2 more than to eubacterial EF-G or other archaebacterial EF-2.
Raimo
G
G
Dipartimento di Biochimica e Biotecnologie Mediche, Università di Napoli Federico II.
Masullo
M
M
Dello Russo
A
A
Parente
A
A
Gambacorta
A
A
Bocchini
V
V
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D010455:Peptides / Q000138:chemical synthesis; D011072:Poly U / Q000378:metabolism; D016944:Sulfolobus / Q000737:chemistry*
D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D010455:Peptides; D000246:Adenosine Diphosphate Ribose; D011072:Poly U; C012001:polyphenylalanine