Rho-modifying C3-like ADP-ribosyltransferases
- PMID: 15372308
- DOI: 10.1007/s10254-004-0034-4
Rho-modifying C3-like ADP-ribosyltransferases
Abstract
C3-like exoenzymes comprise a family of seven bacterial ADP-ribosyltransferases, which selectively modify RhoA, B, and C at asparagine-41. Crystal structures of C3 exoenzymes are available, allowing novel insights into the structure-function relationships of these exoenzymes. Because ADP-ribosylation specifically inhibits the biological functions of the low-molecular mass GTPases, C3 exoenzymes are established pharmacological tools to study the cellular functions of Rho GTPases. Recent studies, however, indicate that the functional consequences of C3-induced ADP-ribosylation are more complex than previously suggested. In the present review the basic properties of C3 exoenzymes are briefly summarized and new findings are reviewed.
Similar articles
-
Exchange of glutamine-217 to glutamate of Clostridium limosum exoenzyme C3 turns the asparagine-specific ADP-ribosyltransferase into an arginine-modifying enzyme.Biochemistry. 2006 Jan 24;45(3):1017-25. doi: 10.1021/bi052253g. Biochemistry. 2006. PMID: 16411778
-
Rho-specific Bacillus cereus ADP-ribosyltransferase C3cer cloning and characterization.Biochemistry. 2003 Aug 19;42(32):9694-702. doi: 10.1021/bi034583b. Biochemistry. 2003. PMID: 12911311
-
C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins.Naunyn Schmiedebergs Arch Pharmacol. 2007 Feb;374(5-6):347-60. doi: 10.1007/s00210-006-0113-y. Epub 2006 Dec 5. Naunyn Schmiedebergs Arch Pharmacol. 2007. PMID: 17146673 Review.
-
Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis.J Mol Biol. 2001 Jan 5;305(1):95-107. doi: 10.1006/jmbi.2000.4292. J Mol Biol. 2001. PMID: 11114250
-
Studies on the active-site structure of C3-like exoenzymes: involvement of glutamic acid in catalysis of ADP-ribosylation.Biochimie. 1995;77(5):326-32. doi: 10.1016/0300-9084(96)88142-9. Biochimie. 1995. PMID: 8527485 Review.
Cited by
-
EhRho1, a RhoA-like GTPase of Entamoeba histolytica, is modified by clostridial glucosylating cytotoxins.Appl Environ Microbiol. 2006 Dec;72(12):7842-8. doi: 10.1128/AEM.01826-06. Epub 2006 Oct 20. Appl Environ Microbiol. 2006. PMID: 17056697 Free PMC article.
-
The Staphylococcus aureus epidermal cell differentiation inhibitor toxin promotes formation of infection foci in a mouse model of bacteremia.Infect Immun. 2010 Aug;78(8):3404-11. doi: 10.1128/IAI.00319-10. Epub 2010 May 17. Infect Immun. 2010. PMID: 20479081 Free PMC article.
-
The NCA-1 and NCA-2 Ion Channels Function Downstream of Gq and Rho To Regulate Locomotion in Caenorhabditis elegans.Genetics. 2017 May;206(1):265-282. doi: 10.1534/genetics.116.198820. Epub 2017 Mar 21. Genetics. 2017. PMID: 28325749 Free PMC article.
-
Clostridial C3 Toxins Target Monocytes/Macrophages and Modulate Their Functions.Front Immunol. 2015 Jun 30;6:339. doi: 10.3389/fimmu.2015.00339. eCollection 2015. Front Immunol. 2015. PMID: 26175735 Free PMC article. Review.
-
Characterization of C3larvinA, a novel RhoA-targeting ADP-ribosyltransferase toxin produced by the honey bee pathogen, Paenibacillus larvae.Biosci Rep. 2020 Jan 31;40(1):BSR20193405. doi: 10.1042/BSR20193405. Biosci Rep. 2020. PMID: 31844879 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous