EC Number   |
General Information |
Reference |
|---|
   3.1.26.4 | evolution |
reverse transcriptase (RT) and ribonuclease H are among the most ancient and abundant protein folds. RNases H may have evolved from ribozymes, related to viroids, early in the RNA world, forming ribosomes, RNA replicases and polymerases. Basic RNA-binding peptides enhance ribozyme catalysis. RT and ribozymes or RNases H are present today in bacterial group II introns, the precedents of transposable elements. Thousands of unique RTs and RNases H are present in eukaryotes, bacteria, and viruses |
750633 |
| 3.1.26.4 | evolution |
ribonuclease H (RNase H) belongs to the nucleotidyl-transferase (NT) superfamily and is a prototypical member of a large family of enzymes that use two-metal ion (Mg2+ or Mn2+) catalysis to cleave nucleic acids |
751190 |
| 3.1.26.4 | evolution |
RNaseH enzymes belong to the nucleotidyl transferase superfamily whose members share a similar protein fold and catalytic mechanism |
749598 |
| 3.1.26.4 | evolution |
the reverse transcriptase (RT) and ribonuclease H are among the most ancient and abundant protein folds. RNases H may have evolved from ribozymes, related to viroids, early in the RNA world, forming ribosomes, RNA replicases and polymerases. Basic RNA-binding peptides enhance ribozyme catalysis. RT and ribozymes or RNases H are present today in bacterial group II introns, the precedents of transposable elements. Thousands of unique RTs and RNases H are present in eukaryotes, bacteria, and viruses |
750633 |
| 3.1.26.4 | malfunction |
deletion of rnhB sensitizes Mycobacterium smegmatis to UV irradiation in stationary phase. DELTArnhA/DELTArnhB cells in stationary phase are sensitized to killing by hydrogen peroxide |
-, 751735 |
| 3.1.26.4 | malfunction |
DELTArnhA and DELTArnhC are synthetically lethal |
-, 751735 |
| 3.1.26.4 | malfunction |
DELTArnhA and DELTArnhC are synthetically lethal. DELTArnhA/DELTArnhB cells in stationary phase are sensitized to killing by hydrogen peroxide |
-, 751735 |
| 3.1.26.4 | malfunction |
disease-causing mutations impairs the process of RNase H1 direction of origin-specific initiation of DNA replication in human mitochondria. Depletion of RNase H1 causes a reduction in mtDNA level. In an RNase H1-deficient patient cell line, the precise initiation of mtDNA replication is lost and DNA synthesis is initiated from multiple sites throughout the mitochondrial control region. Impaired RNase H1 activity changes replication initiation in vivo. Effects of disease causing mutations in RNASEH1, which are associated with adult-onset mitochondrial encephalomyopathy, phenotype and mechanism, overview |
751911 |
| 3.1.26.4 | malfunction |
disrupting the activity of the two enzymes RNase H1 and H2 (rnh1DELTA rnh201DELTA in Saccharomyces cerevisiae) is a useful tool for increasing the persistence of DNA:RNA hybrids and studying the effects of hybrid-induced instability. In the absence of RNase H activity, the levels of hybrids formed at susceptible loci increase dramatically. This increase in hybrids is associated with increased rates of genome instability that include loss of heterozygosity (LOH) events, loss of entire chromosomes, and recombination at the ribosomal locus. rnh1DELTA rnh201DELTA mutants display an increase in Rad52-GFP foci. Cells lacking RNase H1 and H2 have a larger fraction of persistent R-loop induced damage than wild-type cells or cells lacking only one of the RNases H, failure to observe accumulating foci early in the cell cycle, phenotype, overview |
750405 |
| 3.1.26.4 | malfunction |
disruption of the rnhA gene has been reported to increase a basal level of SOS expression in Escherichia coli, probably due to persistence of R-loops on the chromosome |
752184 |
