Involvement of conserved histidine, lysine and tyrosine residues in the mechanism of DNA cleavage by the caspase-3 activated DNase CAD
ISSN: | 1362-4962 |
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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: |
DNA Fragmentation
Biology Article Cell Line law.invention Mice chemistry.chemical_compound law Catalytic Domain Escherichia coli Genetics Animals Humans Histidine Enzyme Inhibitors Tyrosine Cellulose Conserved Sequence chemistry.chemical_classification Nuclease Deoxyribonucleases Lysine Imidazoles Proteins DNA Hydrogen-Ion Concentration Molecular biology Amino acid Amino Acid Substitution Trinitrobenzenesulfonic Acid Biochemistry chemistry Recombinant DNA biology.protein DNA fragmentation Apoptosis Regulatory Proteins Deoxyribonuclease I |
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 |
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