3.1.26.4 12 base pair RNA-DNA hybrid + H2O - 3.1.26.4 DNA-RNA duplex + H2O specific cleavage of the RNA part 3.1.26.4 DNA-RNA hybrid + H2O - 3.1.26.4 DNA-RNA hybrid + H2O strategy for regulating RNA digestion by RNase H by using a light-activated DNA hairpin, overview 3.1.26.4 DNA-RNA hybrid + H2O in the pause of minus strang synthesis, RNAse H degrades the RNA template, with the exception of the polypurine tract sequence, immediately upstream of U3, which serves as a primer for plus-strand synthesis 3.1.26.4 DNA-RNA hybrid duplex + H2O - 3.1.26.4 additional information presence of intrinsic cell-type specific factors affecting the activity and localization of type 2 enzyme 3.1.26.4 additional information the enzyme is regulated by a unique redox switch formed by adjacent Cys147 and Cys148 3.1.26.4 additional information the enzyme is required for kinetoplast DNA replication in the mitochondrion, the RNase HIIC is essential for growth of promastigotes and amastigotes 3.1.26.4 additional information member of the nucleotidyl-transferase superfamily and endo-nucleolytically cleaves the RNA portion in RNA/DNA hybrids and removes RNA primers from Okazaki fragments. Enzyme binds RNA and DNA duplexes but is unable to cleave either 3.1.26.4 additional information ribonuclease H is an enzyme that specifically cleaves RNA of RNA?DNA hybrids 3.1.26.4 additional information RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids 3.1.26.4 additional information RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids. A two-metal ion mechanism requires that metal ion A activates a water molecule as a nucleophile and moves towards ion B, bringing the nucleophile in close proximity to the scissile bond, while metal ion B destabilizes the substrate-enzyme interaction and lowers the energy barrier to product formation 3.1.26.4 additional information RNase H specifically hydrolyzes the RNA strand of RNA/DNA hybrids in the presence of divalent metal ions, such as Mg2+ and Mn2+ 3.1.26.4 additional information RNase H2 hydrolyzes RNA of RNA/DNA hybrids and can nick duplex DNAs containing a single ribonucleotide. It shows a unique mechanism of recognition and substrate-assisted cleavage with preference for junction substrates. A conserved tyrosine residue distorts the nucleic acid at the junction, allowing the substrate to function in catalysis by participating in coordination of the active site metal ion 3.1.26.4 additional information RNases hydrolyze RNA/DNA in the presence of various divalent cofactors such as Mg2+ and Mn2+ 3.1.26.4 additional information the eukaryotic RNase H2 heterotrimeric complex recognizes RNA/DNA hybrids and 5'RNA-DNA3'/DNA junction hybrids as substrates with similar efficiency 3.1.26.4 additional information reconstitution of the replication cycle of L-strand synthesis in vitro using recombinant mitochondrial proteins and model OriL substrates: the process begins with initiation of DNA replication at OriL and ends with primer removal and ligation. RNase H1 partially removes the primer, leaving behind the last one to three ribonucleotides. These 5'-end ribonucleotides disturb ligation and are removed by Flap endonuclease 1 (FEN1) 3.1.26.4 additional information ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function 3.1.26.4 additional information RNase H is a non-specific endonuclease which degrades selectively the RNA strand in DNA/RNA duplexes 3.1.26.4 additional information RNase H1 is an RNase H enzyme capable of cleaving RNA-DNA hybrids. It can cleave hybrids that are down to approximately 6 nucleotides in length. The enzyme can also cleave Okazaki fragment-like structures, leaving approximately two ribonucleotides next to the RNA-DNA junction 3.1.26.4 additional information RNaseH1-dependent antisense oligonucleotides (ASOs) activity in human cells, mechanism and regulation, overview 3.1.26.4 additional information RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes 3.1.26.4 additional information RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA 3.1.26.4 RNA*DNA hybrid + H2O cleaves the RNA portion 3.1.26.4 RNA-DNA heteroduplex + H2O - 3.1.26.4 RNA-DNA hybrid + H2O - 3.1.26.4 RNA-DNA hybrid + H2O RNase H2 incises the DNA 5'-of the ribonucleotide, generating DNA containing 3'-hydroxyl and 5'-phosphoribonucleotide ends 3.1.26.4 RNA-DNA hybrid + H2O the enzyme may play a role in ribonucleotide excision from genomic DNA during replication 3.1.26.4 RNA-DNA hybrid + H2O the enzyme could be involved in the removal of RNA primers during DNA replication 3.1.26.4 RNA-DNA hybrid + H2O RNases H3 recognizes the 2'-OH groups of the RNA strand and detects the DNA strand by binding a phosphate group and inducing B-form conformation 3.1.26.4 RNA-DNA hybrid + H2O the enzyme specifically cleaves the RNA strand of RNA/DNA hybrids 3.1.26.4 RNA-DNA*DNA hybrid + H2O enzyme removes RNA primers from lagging strand fragments during DNA replication, 5'-to 3'-exonuclease activity, degradation of the RNA portion of the duplex 3.1.26.4 RNA-DNA*DNA hybrid + H2O RNA primer recognition and removal during DNA replication 3.1.26.4 RNA-DNA/DNA hybrid + H2O PabRNase HII acts as a specific endonuclease on RNA-DNA/DNA duplexes. Specific cleavage, one nucleotide upstream of the RNA-DNA junction, occurs on a substrate in which RNA initiators is fully annealed to the cDNA template. Additionally, PabRNase HII cleaves a single ribonucleotide embedded in a double-stranded DNA 3.1.26.4 ssDNA-dsDNA + H2O 5'-to 3'-exonuclease activity, exonuclease activity removing short oligonucleotides of 3-30 nucleotides from adjacent DNA