Abstract
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 language | English |
|---|---|
| Pages (from-to) | 127-132 |
| Number of pages | 6 |
| Journal | BBA - Gene Structure and Expression |
| Volume | 1132 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Sep 24 1992 |
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Keywords
- ADP-ribosylation
- Elongation factor 2
- Protein synthesis
- Thermostability
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Genetics
- Structural Biology
Cite this
Molecular, functional and structural properties of an archaebacterial elongation factor 2. / Raimo, Gennaro; Masullo, Mariorosario; Parente, Augusto; Russo, Antonio Dello; Bocchini, Vincenzo.
In: BBA - Gene Structure and Expression, Vol. 1132, No. 2, 24.09.1992, p. 127-132.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular, functional and structural properties of an archaebacterial elongation factor 2
AU - Raimo, Gennaro
AU - Masullo, Mariorosario
AU - Parente, Augusto
AU - Russo, Antonio Dello
AU - Bocchini, Vincenzo
PY - 1992/9/24
Y1 - 1992/9/24
N2 - 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.
AB - 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.
KW - ADP-ribosylation
KW - Elongation factor 2
KW - Protein synthesis
KW - Thermostability
UR - http://www.scopus.com/inward/record.url?scp=0026669687&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026669687&partnerID=8YFLogxK
U2 - 10.1016/0167-4781(92)90002-H
DO - 10.1016/0167-4781(92)90002-H
M3 - Article
C2 - 1390884
AN - SCOPUS:0026669687
VL - 1132
SP - 127
EP - 132
JO - Biochimica et Biophysica Acta - Gene Structure and Expression
JF - Biochimica et Biophysica Acta - Gene Structure and Expression
SN - 0167-4781
IS - 2
ER -