Bacterial protein toxins inhibiting low-molecular-mass GTP-binding proteins

2001 ◽  
Vol 291 (4) ◽  
pp. 243-250 ◽  
Author(s):  
Ingo Just ◽  
Fred Hofmann ◽  
Harald Genth ◽  
Ralf Gerhard
1989 ◽  
Vol 264 (28) ◽  
pp. 16383-16389
Author(s):  
P G Polakis ◽  
R F Weber ◽  
B Nevins ◽  
J R Didsbury ◽  
T Evans ◽  
...  

1991 ◽  
Vol 276 (3) ◽  
pp. 833-836 ◽  
Author(s):  
M D Garrett ◽  
G N Major ◽  
N Totty ◽  
A Hall

Eukaryotic cells contain numerous small-molecular-mass GTP-binding proteins, but the processes that they regulate are not known. Different members of this protein family appear to be associated with specific GTPase-activating proteins (GAPs), and we have previously reported the identification of a cytoplasmic GAP (rho GAP) that stimulates the GTPase activity of p21rho but not of other small-molecular-mass GTP-binding proteins. We have now purified rho GAP 2000-fold from human spleen tissue using f.p.l.c. Electrotransfer of this 27.5 kDa protein on to an Immobilon-P transfer membrane followed by reconstitution of its enzymic activity confirmed its identity. Rho GAP was subjected to N-terminal sequence analysis and 15 amino acids were obtained. The sequence showed 53% identity with a region present in IRA1, a protein which stimulates the GTPase activity of RAS proteins in Saccharomyces cerevisiae. These results suggest that there is a family of sequence-related GAP proteins, which to date includes ras GAP and its yeast counterparts IRA1 and IRA2, rho GAP and the Neurofibromatosis gene product NF1.


FEBS Letters ◽  
1991 ◽  
Vol 291 (2) ◽  
pp. 336-340 ◽  
Author(s):  
Gertrud Koch ◽  
Barbara Haberman ◽  
Christiane Mohr ◽  
Ingo Just ◽  
Klaus Aktories

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