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Example sentences for: nucleases
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Cytochrome c is then released from the mitochondria into the cytosol, where it interacts with downstream proapoptotic proteins such as Apaf-1 and caspase 9. Activation of these proteins further activates nucleases, such as caspase-activated DNase (CAD), which cause DNA fragmentation.
Thus, it appears plausible that these domains evolved from an ancestral nucleic-acid-binding module that, on one hand, gave rise to the nucleases through the acquisition of an amino-terminal helical extension that provided the active site, and on the other hand, diversified into distinct nucleic-acid-binding domains.
This alignment could be extended to the enzymatic core of three characteristic Mg 2+-dependent endonucleases: the bovine DNAseI [ 29 ] and two apurinic/apyrimidinic (AP) DNA-repair endonucleases, i.e. the E. coli Exonuclease III [ 30 ] and the human HAP1 protein [ 31 ] . These nucleases share the same catalytic residues and form a similar four-layered α/β-sandwich motif.
Genes for SSAPs from all the 3 distinct superfamilies may also occur adjacent to or in the vicinity of genes encoding nucleases or Holliday junction resolvases (HJRs).
The RDRPs of RNA viruses define one major lineage of nucleic acid polymerases, which additionally includes reverse transcriptases, archaeo-eukaryotic DNA polymerases, and nucleotide cyclases [ 8 9 10 11 12 13 ] . The DNA-dependent RNA polymerase of certain bacteriophages, such as T7, and the archaeo-eukaryotic primase (also detected in some bacteria) are divergent derivatives of the same fold [ 11 14 ] . The core catalytic domain of all these enzymes, the so-called "palm" domain, has an RNA-recognition motif (RRM)-like fold with strategically placed metal-coordinating residues, which form the active site [ 11 15 16 ] . In contrast, bacterial DnaG-type primases (also present in archaea and some eukaryotes) contain a polymerase domain of the Rossmann-like TOPRIM fold, which is shared with topoisomerases and OLD-family nucleases [ 17 18 19 ] . The recently solved structures of the DDRPs from yeast and the thermophilic bacterium Thermus thermophilus indicate that the β' subunit (according to the subunit nomenclature of Escherichia coli DDRP, which we hereinafter employ to designate all orthologs of the respective E. coli subunits) of these enzymes defines another distinct catalytic scaffold, which is unrelated to any of the above template-dependent RNA polymerases [ 20 21 22 23 24 ] . Additionally, the structural and evolutionary affinities of two other template-dependent RNA polymerases, namely RDRPs involved in PTGS [ 25 26 27 ] and primases of herpesviruses [ 28 ] , remain obscure.
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