Cloned (Comment) | Organism |
---|---|
Expression of the N-terminally His6-tagged mutant Galphai/q chimeric gene, in which the native N-terminus of Galphaq is replaced with that of Galphai1, the gene also posseses a TEV cleavage site, amino acids 1-28 of rat Galphai1, a linker of Arg and Ser, and the 37-359 amino acid region of mouse Galphaq, expression of recombinant wild-type Galphaq and Galphaq mutant Q209E in Mus musculus Galphaq/11-deficient embryonic fibroblasts, Swiss3T3 cells, expression of alpha subunit cDNAs of heterotrimeric GTPases, Gs, Gi-2, G13 and G11 in human 293T cells | Pasteurella multocida |
Protein Variants | Comment | Organism |
---|---|---|
Q209E | a Galphaq mutant, constructed for rasing of antibodies that specifically detect PMT-deaminated GTPase Galphaq | Pasteurella multocida |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pasteurella multocida | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
G12 | - |
Pasteurella multocida |
G13 | - |
Pasteurella multocida |
GI | - |
Pasteurella multocida |
Gq | - |
Pasteurella multocida |
heterotrimeric GTPase | - |
Pasteurella multocida |
General Information | Comment | Organism |
---|---|---|
physiological function | the virulence factor and highly potent mitogen Pasteurella multocida toxin, PMT, exhibits its toxic activity through activation of heterotrimeric GTPase-dependent pathways, by deamidating a glutamine residue in the alpha subunit of these GTPases via its C-terminal C3 domain, mechanism, overview. Galpha11 and Galphaq are substrates for PMT. C-PMT deamidates Galphaq at least tenfold more efficiently than the full-length PMT. Mutant PMT C1165S is not active on the GTPases, while the mutant C-terminal part of PMT C1159S deamidates Gai/q | Pasteurella multocida |