Decoding the Logic of the tRNA Regiospecificity of Nonribosomal FemXWv Aminoacyl Transferase

2010 ◽  
Vol 122 (30) ◽  
pp. 5241-5245 ◽  
Author(s):  
Matthieu Fonvielle ◽  
Maryline Chemama ◽  
Maxime Lecerf ◽  
Régis Villet ◽  
Patricia Busca ◽  
...  
1966 ◽  
Vol 241 (8) ◽  
pp. 1698-1704
Author(s):  
Richard P. Sutter ◽  
Kivie Moldave

2010 ◽  
Vol 49 (30) ◽  
pp. 5115-5119 ◽  
Author(s):  
Matthieu Fonvielle ◽  
Maryline Chemama ◽  
Maxime Lecerf ◽  
Régis Villet ◽  
Patricia Busca ◽  
...  

1972 ◽  
Vol 152 (2) ◽  
pp. 451-456 ◽  
Author(s):  
Richard E. Gregg ◽  
Roger L. Heintz

1970 ◽  
Vol 132 (6) ◽  
pp. 1138-1152 ◽  
Author(s):  
Joel B. Baseman ◽  
A. M. Pappenheimer ◽  
D. M. Gill ◽  
Annabel A. Harper

The blood clearance and distribution in the tissues of 125I after intravenous injection of small doses (1.5–5 MLD or 0.08–0.25 µg) of 125I-labeled diphtheria toxin has been followed in guinea pigs and rabbits and compared with the fate of equivalent amounts of injected 125I-labeled toxoid and bovine serum albumin. Toxoid disappeared most rapidly from the blood stream and label accumulated and was retained in liver, spleen, and especially in kidney. Both toxin and BSA behaved differently. Label was found widely distributed among all the organs except the nervous system and its rate of disappearance from the tissues paralleled its disappearance from the circulation. There was no evidence for any particular affinity of toxin for muscle tissue or for a "target" organ. Previous reports by others that toxin causes specific and selective impairment of protein synthesis in muscle tissue were not confirmed. On the contrary, both in guinea pigs and rabbits, a reduced rate of protein synthesis was observed in all tissues that had taken up the toxin label. In tissues removed from intoxicated animals of both species there was an associated reduction in aminoacyl transferase 2 content. It is concluded that the primary action of diphtheria toxin in the living animal is to effect the inactivation of aminoacyl transferase 2. The resulting inhibition in rate of protein synthesis leads to morphologic damage in all tissues reached by the toxin and ultimately to death of the animal.


1970 ◽  
Vol 45 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Emma Shelton ◽  
Edward L. Kuff ◽  
Elizabeth S. Maxwell ◽  
J. T. Harrington

It has been possible to show by electron microscopy of samples selected from sucrose gradients that particles of specific size and shape are present in supernatant fluids derived from nucleated animal and plant cells, but not in extracts from Escherichia coli. Aminoacyl transferase I activity in these same gradients sediments in two peaks representing material of approximately 5–7S and 18–20S. A rectangular particle, 100 x 145 A in size, sediments at 19S and coincides with the second peak of transferase I activity. The possibility that the rectangular particle may be a "carrier" particle associated with transferase I is discussed.


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