Characterization of diphtheria-toxin-resistant mutants lacking receptor function or containing nonribosylatable elongation factor 2

1985 ◽  
Vol 11 (5) ◽  
pp. 421-431 ◽  
Author(s):  
Kenji Kohno ◽  
Tsuyoshi Uchida ◽  
Eisuke Mekada ◽  
Yoshio Okada
Keyword(s):  
Diphtheria Toxin ◽  
Elongation Factor ◽  
Receptor Function ◽  
Elongation Factor 2 ◽  
Resistant Mutants

scholarly journals Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling.

1992 ◽  
Vol 267 (2) ◽  
pp. 1190-1197 ◽  
Author(s):  
J P Perentesis ◽  
L D Phan ◽  
W B Gleason ◽  
D C LaPorte ◽  
D M Livingston ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Elongation Factor ◽  
Domain Modeling ◽  
Elongation Factor 2

In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin

1984 ◽  
Vol 4 (4) ◽  
pp. 642-650
Author(s):  
T J Moehring ◽  
D E Danley ◽  
J M Moehring
Keyword(s):  
Chinese Hamster Ovary ◽  
Diphtheria Toxin ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Elongation Factor ◽  
Synthetase Activity ◽  
Post Translational Modification ◽  
Ovary Cells ◽  
Elongation Factor 2

Diphthamide, a unique amino acid, is a post-translational derivative of histidine that exists in protein synthesis elongation factor 2 at the site of diphtheria toxin-catalyzed ADP-ribosylation of elongation factor 2. We investigated steps in the biosynthesis of diphthamide with mutants of Chinese hamster ovary cells that were altered in different steps of this complex post-translational modification. Biochemical evidence indicates that this modification requires a minimum of three steps, two of which we accomplished in vitro. We identified a methyltransferase activity that transfers methyl groups from S-adenosyl methionine to an unmethylated form of diphthine (the deamidated form of diphthamide), and we tentatively identified an ATP-dependent synthetase activity involved in the biosynthesis of diphthamide from diphthine. Our results are in accord with the proposed structure of diphthamide (B. G. VanNess, et al., J. Biol. Chem. 255:10710-10716, 1980).

scholarly journals Purification and characterization of native human elongation factor 2

2019 ◽  
Vol 158 ◽  
pp. 15-19
Author(s):  
Rasmus Kock Flygaard ◽  
Beatrice Malacrida ◽  
Patrick Kiely ◽  
Lasse Bohl Jenner
Keyword(s):  
Elongation Factor ◽  
Purification And Characterization ◽  
Elongation Factor 2 ◽  
Human Elongation Factor

Molecular cloning and characterization of a Cryptosporidium parvum elongation factor-2 gene

1995 ◽  
Vol 71 (1) ◽  
pp. 143-147 ◽  
Author(s):  
Douglas E. Jones ◽  
Tu D. Tu ◽  
Sameer Mathur ◽  
Raymond W. Sweeney ◽  
Douglas P. Clark
Keyword(s):  
Molecular Cloning ◽  
Cryptosporidium Parvum ◽  
Elongation Factor ◽  
Elongation Factor 2

Eukaryotic elongation factor-2 (eEF-2) activity in bovine mammary tissue in relation to milk protein synthesis

2002 ◽  
Vol 69 (2) ◽  
pp. 205-212 ◽  
Author(s):  
CLAUS T. CHRISTOPHERSEN ◽  
JAKOB KARLSEN ◽  
METTE O. NIELSEN ◽  
BENT RIIS
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Mammary Gland ◽  
Diphtheria Toxin ◽  
Milk Protein ◽  
Elongation Factor ◽  
Mammary Tissue ◽  
Limiting Factor ◽  
Elongation Factor 2 ◽  
High Level

The amount of protein synthesis translational elongation factor 2 (eEF-2) was estimated employing diphtheria toxin-dependent ADP-ribosylation in samples prepared from small amounts of tissue from mammary gland, skeletal muscle and liver from lactating dairy cows. A very high level of ADP-ribosylatable eEF-2 was found in mammary gland, amounting to 20-times the level found in liver and 50-times the level found in skeletal muscle. This obviously reflects the high protein synthesis activity in mammary tissue. To our knowledge, similar high activities have previously been reported only for cancer cells. A close linear relationship was found between the amount of diphtheria-toxin catalysed ADP-ribosylated eEF-2 and protein and casein output in milk from cows in late lactation. This strongly suggests that eEF-2 may be a limiting factor in milk protein synthesis.

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