Structural dynamics of the complex of calmodulin with a minimal functional construct of eukaryotic elongation factor 2 kinase and the role of Thr348 autophosphorylation

2021 ◽  
Author(s):  
Andrea Piserchio ◽  
Kimberly Long ◽  
Kwangwoon Lee ◽  
Eric A. Kumar ◽  
Rinat Abzalimov ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Elongation Factor ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor

The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A

2008 ◽  
Vol 413 (1) ◽  
pp. 163-174 ◽  
Author(s):  
Yong Zhang ◽  
Suya Liu ◽  
Gilles Lajoie ◽  
A. Rod Merrill
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Elongation Factor ◽  
Exotoxin A ◽  
Mutant Proteins ◽  
Adp Ribosylation ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor ◽  
Pseudomonas Aeruginosa Exotoxin

eEF2 (eukaryotic elongation factor 2) contains a post-translationally modified histidine residue, known as diphthamide, which is the specific ADP-ribosylation target of diphtheria toxin, cholix toxin and Pseudomonas aeruginosa exotoxin A. Site-directed mutagenesis was conducted on residues within the diphthamide-containing loop (Leu693–Gly703) of eEF2 by replacement with alanine. The purified yeast eEF2 mutant proteins were then investigated to determine the role of this loop region in ADP-ribose acceptor activity of elongation factor 2 as catalysed by exotoxin A. A number of single alanine substitutions in the diphthamide-containing loop caused a significant reduction in the eEF2 ADP-ribose acceptor activities, including two strictly conserved residues, His694 and Asp696. Analysis by MS revealed that all of these mutant proteins lacked the 2′-modification on the His699 residue and that eEF2 is acetylated at Lys509. Furthermore, it was revealed that the imidazole ring of Diph699 (diphthamide at position 699) still functions as an ADP-ribose acceptor (albeit poorly), even without the diphthamide modification on the His699. Therefore, this diphthamide-containing loop plays an important role in the ADP-ribosylation of eEF2 catalysed by toxin and also for modification of His699 by the endogenous diphthamide modification machinery.

scholarly journals The role of calcium in the interaction between calmodulin and a minimal functional construct of eukaryotic elongation factor 2 kinase

2019 ◽  
Vol 28 (12) ◽  
pp. 2089-2098
Author(s):  
Kwangwoon Lee ◽  
Eric A. Kumar ◽  
Kevin N. Dalby ◽  
Ranajeet Ghose
Keyword(s):  
Elongation Factor ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor

Flavonoids from Deguelia duckeana inhibit the eukaryotic elongation factor 2 (eEF2) in SK-N-SH neuronal cells

Planta Medica ◽  
2015 ◽  
Vol 81 (16) ◽  
Author(s):  
LMC Cursino ◽  
NM Lima ◽  
R Murillo ◽  
I Merfort ◽  
M Humar ◽  
...  
Keyword(s):  
Neuronal Cells ◽  
Elongation Factor ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor

Effect of oxidative stress on in vivo ADP-ribosylation of eukaryotic elongation factor 2

2005 ◽  
Vol 37 (1) ◽  
pp. 91-99 ◽  
Author(s):  
Muhammet Bektaş ◽  
Handan Akçakaya ◽  
Aysin Aroymak ◽  
Rüstem Nurten ◽  
Engin Bermek
Keyword(s):  
Oxidative Stress ◽  
Elongation Factor ◽  
Adp Ribosylation ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor

scholarly journals Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2

2019 ◽  
Vol 74 (1) ◽  
pp. 88-100.e9 ◽  
Author(s):  
Leonie Mönkemeyer ◽  
Courtney L. Klaips ◽  
David Balchin ◽  
Roman Körner ◽  
F. Ulrich Hartl ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Chaperone Function ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor
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