Superfluous glutamine synthetase activity in Chinese Hamster Ovary cells selected under glutamine limitation is growth limiting in glutamine‐replete conditions and can be inhibited by serine

2019 ◽  
Vol 35 (5) ◽  
Author(s):  
Vishwanathgouda Maralingannavar ◽  
Dharmeshkumar Parmar ◽  
Venkateswarlu Panchagnula ◽  
Mugdha Gadgil
Keyword(s):  
Glutamine Synthetase ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Synthetase Activity ◽  
Glutamine Synthetase Activity ◽  
Ovary Cells ◽  
Glutamine Limitation

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).

Effect of culture temperature on TNFR-Fc productivity in recombinant glutamine synthetase-chinese hamster ovary cells

2010 ◽  
Vol 32 (9) ◽  
pp. 1239-1244 ◽  
Author(s):  
Li Fan ◽  
Liang Zhao ◽  
Zhaoyang Ye ◽  
Yating Sun ◽  
Tianci Kou ◽  
...  
Keyword(s):  
Glutamine Synthetase ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Culture Temperature ◽  
Ovary Cells

scholarly journals 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).

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