Involvement of conserved histidine, lysine and tyrosine residues in the mechanism of DNA cleavage by the caspase-3 activated DNase CAD

Asp/Glu or Arg exchanges lead to variants with -->
ISSN: 1362-4962
Přístupová URL adresa: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d051eb6892c117c5e7bd5a843db3b6a8
https://doi.org/10.1093/nar/30.6.1325
Rights: OPEN
Přírůstkové číslo: edsair.doi.dedup.....d051eb6892c117c5e7bd5a843db3b6a8
Autor: Christian Korn, Sebastian Richard Scholz, Gregor Meiss, Alfred Pingoud, Oleg Gimadutdinow
Rok vydání: 2002
Předmět:
Zdroj: Nucleic Acids Research. 30:1325-1332
ISSN: 1362-4962
Popis: The caspase-activated DNase (CAD) is involved in DNA degradation during apoptosis. Chemical modification of murine CAD with the lysine-specific reagent 2,4,6-trinitrobenzenesulphonic acid and the tyrosine-specific reagent N-acetylimidazole leads to inactivation of the nuclease, indicating that lysine and tyrosine residues are important for DNA cleavage by this enzyme. The presence of DNA or the inhibitor ICAD-L protects the enzyme from modification. Amino acid substitution in murine CAD of lysines and tyrosines conserved in CADs from five different species leads to variants with little if any catalytic activity, but unaltered DNA binding (K155Q, K301Q, K310Q, Y247F), with the exception of Y170F, which retains wild-type activity. Similarly, as observed for the previously characterised H242N, H263N, H308N and H313N variants, the newly introduced His-->Asp/Glu or Arg exchanges lead to variants with
Databáze: OpenAIRE