Transfer RNA-Dependent Aminolevulinic Acid Formation: Structure and Function Of Glutamyl-tRNA Synthetase, Reductase and Glutamate-1-Semialdehyde-2,1-Aminomutase

2007 ◽  
pp. 159-171 ◽  
Author(s):  
Dieter Jahn ◽  
Jürgen Moser ◽  
Wolf-Dieter Schubert ◽  
Dirk W. Heinz
Keyword(s):  
Aminolevulinic Acid ◽  
Trna Synthetase ◽  
Transfer Rna ◽  
Structure And Function ◽  
Acid Formation ◽  
And Function

Structure and function of glutamyl-tRNA reductase involved in 5-aminolevulinic acid formation

2002 ◽  
Vol 30 (3) ◽  
pp. A47-A47
Author(s):  
J. Moser ◽  
W.-D. Schubert ◽  
D. Heinz ◽  
D. Jahn
Keyword(s):  
Aminolevulinic Acid ◽  
Structure And Function ◽  
Acid Formation ◽  
And Function

scholarly journals Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation

2016 ◽  
Vol 291 (33) ◽  
pp. 17102-17111 ◽  
Author(s):  
Chih-Yao Chang ◽  
Chia-Pei Chang ◽  
Shruti Chakraborty ◽  
Shao-Win Wang ◽  
Yi-Kuan Tseng ◽  
...  
Keyword(s):  
Trna Synthetase ◽  
Structure And Function ◽  
Yeast Culture ◽  
Obvious Effect ◽  
Heat Stable ◽  
Natural Target ◽  
Response To Temperature ◽  
And Function ◽  
Trna Binding

Arc1p is a yeast-specific tRNA-binding protein that forms a ternary complex with glutamyl-tRNA synthetase (GluRSc) and methionyl-tRNA synthetase (MetRS) in the cytoplasm to regulate their catalytic activities and subcellular distributions. Despite Arc1p not being involved in any known biotin-dependent reaction, it is a natural target of biotin modification. Results presented herein show that biotin modification had no obvious effect on the growth-supporting activity, subcellular distribution, tRNA binding, or interactions of Arc1p with GluRSc and MetRS. Nevertheless, biotinylation of Arc1p was temperature dependent; raising the growth temperature from 30 to 37 °C drastically reduced its biotinylation level. As a result, Arc1p purified from a yeast culture that had been grown overnight at 37 °C was essentially biotin free. Non-biotinylated Arc1p was more heat stable, more flexible in structure, and more effective than its biotinylated counterpart in promoting glutamylation activity of the otherwise inactive GluRSc at 37 °C in vitro. Our study suggests that the structure and function of Arc1p can be modulated via biotinylation in response to temperature changes.

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