TY - JOUR
T1 - Divergent effects of fluoroaluminates on the peptide chain elongation factors EF-Tu and EF-G as members of the GTPase superfamily
AU - Mesters, Jeroen R.
AU - de Graaf, J. Martien
AU - Kraal, Barend
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1993/4/26
Y1 - 1993/4/26
N2 - Fluoroaluminates are thought to mimic the γ-phosphate of GTP and thus, together with GDP, perturb the functioning of heterotrimeric GTP-binding G-proteins. Here we show they do inhibit the ribosome-stimulated GTPase activity of EF-G from Escherichia coli via the formation of a stable complex with EF-G·GDP and ribosomes. In contrast, no perturbed interactions were observed in a similar ribosomal complex with EF-Tu. Interestingly, in the absence of ribosomes both EF-Tu and EF-G remain totally unaffected by fluoroaluminates. For members of the GTPase superfamily such differential effects have not been described before.
AB - Fluoroaluminates are thought to mimic the γ-phosphate of GTP and thus, together with GDP, perturb the functioning of heterotrimeric GTP-binding G-proteins. Here we show they do inhibit the ribosome-stimulated GTPase activity of EF-G from Escherichia coli via the formation of a stable complex with EF-G·GDP and ribosomes. In contrast, no perturbed interactions were observed in a similar ribosomal complex with EF-Tu. Interestingly, in the absence of ribosomes both EF-Tu and EF-G remain totally unaffected by fluoroaluminates. For members of the GTPase superfamily such differential effects have not been described before.
UR - http://www.scopus.com/inward/record.url?scp=0027461129&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(93)80097-E
DO - 10.1016/0014-5793(93)80097-E
M3 - Journal articles
C2 - 8477844
AN - SCOPUS:0027461129
SN - 0014-5793
VL - 321
SP - 149
EP - 152
JO - FEBS Letters
JF - FEBS Letters
IS - 2-3
ER -