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PMID: 2492192 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3.

Biochemical and biophysical research communications ·Vol. 158 ·No. 1 ·1989-01-16 ·Pages 209-13

Aktories K, Braun U, Rösener S, Just I, Hall A

Abstract

The ras-related rho A protein expressed in E. coli, was ADP-ribosylated by botulinum ADP-ribosyltransferase C3. C3 also modified the valine-14 mutant rho protein but not the products of H-ras, R-ras, ral, ypt, and rap 1 genes. A ras-rho chimaera consisting of 60 amino acids from the amino terminus of ras fused to 133 amino acids from the carboxy terminus of rho was not modified by C3. Antibodies raised against the porcine brain cytosolic substrate of C3 cross reacted with the rho, valine-14 rho and ras-rho proteins, but not with the gene products of H-ras, R-ras, ral or rap 1. Polyclonal anti-H-ras antibodies cross reacted with H-ras but not with ral, rho, or the C3 substrate purified from porcine brain.

MeSH Terms
ADP Ribose Transferases/metabolism Botulinum Toxins Clostridium botulinum/enzymology Escherichia coli/genetics GTP-Binding Proteins/genetics,metabolism Membrane Proteins/genetics,metabolism Proto-Oncogene Proteins/metabolism Proto-Oncogene Proteins p21(ras) Recombinant Proteins/metabolism Substrate Specificity rhoA GTP-Binding Protein
Chemicals
Membrane Proteins Proto-Oncogene Proteins Recombinant Proteins ADP Ribose Transferases exoenzyme C3, Clostridium botulinum Botulinum Toxins GTP-Binding Proteins Proto-Oncogene Proteins p21(ras) rhoA GTP-Binding Protein
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Aktories K
Rudolf-Buchheim-Institut für Pharmakologie, Giessen, FRG.
Braun U
Rösener S
Just I
Hall A
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1989-01-16
Pages
209-13
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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