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Apoptosis‐related Functional Features of the DNaseI‐like Family of Nucleases
Author(s) -
LIU QING Y.,
RIBECCO MARIA,
PANDEY SIYARAM,
WALKER P. ROY,
SIKORSKA MARIANNA
Publication year - 1999
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1999.tb07922.x
Subject(s) - dna , exonuclease , biology , polymerase , nucleic acid , dna polymerase , dna damage , biochemistry , oligonucleotide , microbiology and biotechnology , amino acid , nuclease , rnase p , genetics , rna , gene
Rat DNaseY b and its human homolog DHP2 are members of a new family of DNaseI‐like endonucleases. They contain all the conserved amino acid residues to engage a DNaseI‐like catalytic activity and the same molecular mechanisms of DNA hydrolysis. The sequence similarity can be extended to other families of nucleases, such as FEN‐1, DNA polymerases, RNaseH and exonuclease III, involved in the ion‐dependent hydrolysis of nucleic acids. Their unique features include the NLS signals that place them in the nucleic and a high content of positively charged amino acid residues that results in their high affinity for the substrate. Their properties are consistent with a role in the early stage DNA degradation during apoptosis. The caspase‐DFF45/CIDE‐CPAN pathway is most likely involved in the second stage of internucleosomal DNA degradation. However, cells express constitutively multiple transcripts encoding DNA degrading enzymes and related molecules, hence they have the molecular diversity to engage the self‐destructive pathway appropriate to a given trigger.