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- W2018741337 abstract "Abstract Clostridium botulinum C3 is the prototype of the family of the C3-like transferases that ADP-ribosylate exclusively RhoA, -B and -C. The ADP-ribose at Asn-41 results in functional inactivation of Rho reflected by disaggregation of the actin cytoskeleton. We report on a new C3-like transferase produced by a pathogenic Staphylococcus aureus strain. The transferase designated C3Stau was cloned from the genomic DNA. At the amino acid level, C3Stau revealed an identity of 35% to C3 from C. botulinum and Clostridium limosumexoenzyme, respectively, and of 78% to EDIN from S. aureus. In addition to RhoA, which is the target of the other C3-like transferases, C3Stau modified RhoE and Rnd3. RhoE was ADP-ribosylated at Asn-44, which is equivalent to Asn-41 of RhoA. RhoE and Rnd3 are members of the Rho subfamily, which are deficient in intrinsic GTPase activity and possess a RhoA antagonistic cell function. The protein substrate specificity found with recombinant Rho proteins was corroborated by expression of RhoE in Xenopus laevis oocytes showing that RhoE was also modified in vivo by C3Stau but not by C3 from C. botulinum. The poor cell accessibility of C3Stau was overcome by generation of a chimeric toxin recruiting the cell entry machinery of C. botulinum C2 toxin. The chimeric C3Stau caused the same morphological and cytoskeletal changes as the chimeric C. botulinum C3. C3Stauis a new member of the family of the C3-like transferases but is also the prototype of a subfamily of RhoE/Rnd modifying transferases." @default.
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- W2018741337 date "2001-03-01" @default.
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- W2018741337 title "A Novel C3-like ADP-ribosyltransferase fromStaphylococcus aureus Modifying RhoE and Rnd3" @default.
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- W2018741337 doi "https://doi.org/10.1074/jbc.m011035200" @default.
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