Cell ablation using wild-type and cold-sensitive ricin-a chain indrosophila embryonic mesoderm

genesis ◽  
2002 ◽  
Vol 34 (1-2) ◽  
pp. 132-134 ◽  
Author(s):  
Marcus J. Allen ◽  
Cahir J. O'Kane ◽  
Kevin G. Moffat
1989 ◽  
Vol 8 (1) ◽  
pp. 301-308 ◽  
Author(s):  
M. J. May ◽  
M. R. Hartley ◽  
L. M. Roberts ◽  
P. A. Krieg ◽  
R. W. Osborn ◽  
...  

2014 ◽  
Vol 460 (1) ◽  
pp. 59-69 ◽  
Author(s):  
Przemysław Grela ◽  
Xiao-Ping Li ◽  
Marek Tchórzewski ◽  
Nilgun E. Tumer

Wild-type yeast ribosomes and ribosomes bearing only the P1B–P2A dimer bound to the ricin A chain better and were more susceptible to depurination and toxicity than ribosomes bearing only the P1A–P2B dimer, indicating that the two stalk dimers differ in their function.


Development ◽  
1992 ◽  
Vol 114 (3) ◽  
pp. 681-687 ◽  
Author(s):  
K.G. Moffat ◽  
J.H. Gould ◽  
H.K. Smith ◽  
C.J. O'Kane

We have developed a system for temperature-inducible killing of specific cells in the fruitfly Drosophila melanogaster. The system overcomes many of the limitations of existing cell ablation methods and is in principle applicable to any non-homeothermic eukaryote. Temperature-sensitive and cold-sensitive mutations in the ricin toxin A chain (RTA) of castor bean were generated in yeast. One cold-sensitive mutation, RAcs2, produced temperature-dependent ablation of eye cells in Drosophila when expressed under control of the eye-specific sev enhancer. At 29 degrees C, cell death was observed within 7 hours in the developing eye and no obvious toxic effects were observed elsewhere; at 18 degrees C, extremely low toxicity was observed. DNA sequencing of RAcs2 revealed a single amino acid substitution in the RTA active site cleft.


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