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Mol Cell Biol. 1988 Jan;8(1):418-26.

Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum.

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  • 1Department of Molecular Biology and Microbiology, School of Medicine, Tufts University, Boston, Massachusetts 02111.


Exoenzyme C3 from Clostridium botulinum types C and D specifically ADP-ribosylated a 21-kilodalton cellular protein, Guanyl nucleotides protected the substrate against denaturation, which implies that is a G protein. When introduced into the interior of cells, purified exoenzyme C3 ADP-ribosylated intracellular and changed its function. NIH 3T3, PC12, and other cells rapidly underwent temporary morphological alterations that were in certain respects similar to those seen after microinjection of cloned ras proteins. When injected into Xenopus oocytes, C3 induced migration of germinal vesicles and potentiated the cholera toxin-sensitive augmentation of germinal vesicle breakdown by progesterone, also as caused by ras proteins. Nevertheless, was immunologically distinct from p21ras.

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