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Literature summary extracted from
- Division of labor among Mycobacterium smegmatis RNase H enzymes RNase H1 activity of RnhA or RnhC is essential for growth whereas RnhB and RnhA guard against killing by hydrogen peroxide in stationary phase (2017), Nucleic Acids Res., 45, 1-14 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | drug development | RnhC in pathogenic mycobacteria is a possible candidate drug discovery target for tuberculosis and leprosy | Mycolicibacterium smegmatis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.26.4 | gene rnhA, recombinant expression of wild-type and mutant His10-tagged enzymes in Escherichia coli | Mycolicibacterium smegmatis |
| 3.1.26.4 | gene rnhB | Mycolicibacterium smegmatis |
| 3.1.26.4 | gene rnhC | Mycolicibacterium smegmatis |
| 3.1.26.4 | gene rnhD | Mycolicibacterium smegmatis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | D72N | site-directed mutagenesis, a conservative substitution at the metal binding site that abolishes the magnesium-dependent nuclease activity | Mycolicibacterium smegmatis |
| 3.1.26.4 | E50Q | site-directed mutagenesis, a conservative substitution at the metal binding site that abolishes the magnesium-dependent nuclease activity | Mycolicibacterium smegmatis |
| 3.1.26.4 | additional information | deletion of gene rnhA, additional deletions of rnhB, rnhC, and rnhD genes, genotyping of DELTArnh mutants and phenotypes, overview. DELTArnhA and DELTArnhC are synthetically lethal. DELTArnhA/DELTArnhB cells in stationary phase are sensitized to killing by hydrogen peroxide, the DELTArnhA/DELTArnhB/DELTArnhD mutant is about 17fold more sensitive than wild-type to killing in log phase by 20 mM H2O2 | Mycolicibacterium smegmatis |
| 3.1.26.4 | additional information | deletion of gene rnhB, additional deletions of rnhA, rnhC, and rnhD genes, genotyping of DELTArnh mutants and phenotypes, overview. DELTArnhA/DELTArnhB cells in stationary phase are sensitized to killing by hydrogen peroxide. The DELTArnhA/DELTArnhB double mutant is more sensitive than DELTArnhB to killing by UV in stationary phase, and the DELTArnhA/DELTArnhB/DELTArnhD mutant is about 17fold more sensitive than wild-type to killing in log phase by 20 mM H2O2 | Mycolicibacterium smegmatis |
| 3.1.26.4 | additional information | deletion of gene rnhC, additional deletions of rnhB, rnhA, and rnhD genes, genotyping of DELTArnh mutants and phenotypes, overview. DELTArnhA and DELTArnhC are synthetically lethal | Mycolicibacterium smegmatis |
| 3.1.26.4 | additional information | deletion of gene rnhD, additional deletions of rnhB, rnhC, and rnhA genes, genotyping of DELTArnh mutants and phenotypes, overview. The DELTArnhA/DELTArnhB/DELTArnhD mutant is about 17fold more sensitive than wild-type to killing in log phase by 20 mM H2O2 | Mycolicibacterium smegmatis |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.4 | Mg2+ | dependent on | Mycolicibacterium smegmatis |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.4 | additional information | Mycolicibacterium smegmatis | 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 | Mycolicibacterium smegmatis | 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 | additional information | Mycolicibacterium smegmatis ATCC 700084 | 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 | Mycolicibacterium smegmatis ATCC 700084 | 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 | additional information | Mycolicibacterium smegmatis mc(2)155 | 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 | Mycolicibacterium smegmatis mc(2)155 | 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 | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.4 | Mycolicibacterium smegmatis | - |
- |
- |
| 3.1.26.4 | Mycolicibacterium smegmatis | A0QV44 | - |
- |
| 3.1.26.4 | Mycolicibacterium smegmatis | A0R3Q8 | - |
- |
| 3.1.26.4 | Mycolicibacterium smegmatis ATCC 700084 | - |
- |
- |
| 3.1.26.4 | Mycolicibacterium smegmatis ATCC 700084 | A0QV44 | - |
- |
| 3.1.26.4 | Mycolicibacterium smegmatis ATCC 700084 | A0R3Q8 | - |
- |
| 3.1.26.4 | Mycolicibacterium smegmatis mc(2)155 | - |
- |
- |
| 3.1.26.4 | Mycolicibacterium smegmatis mc(2)155 | A0QV44 | - |
- |
| 3.1.26.4 | Mycolicibacterium smegmatis mc(2)155 | A0R3Q8 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.26.4 | recombinant wild-type and mutant His10-tagged enzymes from Escherichia coli by nickel affinity chromatography and gel filtration | Mycolicibacterium smegmatis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 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 | Mycolicibacterium smegmatis | ? | - |
? | |
| 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 | Mycolicibacterium smegmatis | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand | Mycolicibacterium smegmatis | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview | Mycolicibacterium smegmatis | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview | Mycolicibacterium smegmatis | ? | - |
? | |
| 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 | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? | |
| 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 | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? | |
| 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 | Mycolicibacterium smegmatis mc(2)155 | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview | Mycolicibacterium smegmatis mc(2)155 | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview | Mycolicibacterium smegmatis mc(2)155 | ? | - |
? | |
| 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 | Mycolicibacterium smegmatis mc(2)155 | ? | - |
? | |
| 3.1.26.4 | additional information | RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand | Mycolicibacterium smegmatis mc(2)155 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | ? | x * 18000, recombinant His10-tagged enzyme, SDS-PAGE | Mycolicibacterium smegmatis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | RNase H1 | - |
Mycolicibacterium smegmatis |
| 3.1.26.4 | rnhA | - |
Mycolicibacterium smegmatis |
| 3.1.26.4 | RnhB | - |
Mycolicibacterium smegmatis |
| 3.1.26.4 | rnhC | - |
Mycolicibacterium smegmatis |
| 3.1.26.4 | rnhD | - |
Mycolicibacterium smegmatis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 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 | Mycolicibacterium smegmatis |
| 3.1.26.4 | malfunction | DELTArnhA and DELTArnhC are synthetically lethal | Mycolicibacterium smegmatis |
| 3.1.26.4 | malfunction | DELTArnhA and DELTArnhC are synthetically lethal. DELTArnhA/DELTArnhB cells in stationary phase are sensitized to killing by hydrogen peroxide | Mycolicibacterium smegmatis |
| 3.1.26.4 | physiological function | RNase H1 activity is essential for mycobacterial growth and can be provided by either RnhC or RnhA. The RNase H2 enzymes RnhB and RnhD are dispensable for growth. RnhB and RnhA collaborate to protect Mycobacterium smegmatis against oxidative damage in stationary phase | Mycolicibacterium smegmatis |
| 3.1.26.4 | physiological function | RnhA like RnhC is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. RNase H1 activity is essential for mycobacterial growth and can be provided by either RnhC or RnhA. The RNase H2 enzymes RnhB and RnhD are dispensable for growth. RnhB and RnhA collaborate to protect Mycobacterium smegmatis against oxidative damage in stationary phase | Mycolicibacterium smegmatis |
| 3.1.26.4 | physiological function | RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. RNase H1 activity is essential for mycobacterial growth and can be provided by either RnhC or RnhA. The RNase H2 enzymes RnhB and RnhD are dispensable for growth. RnhB and RnhA collaborate to protect Mycobacterium smegmatis against oxidative damage in stationary phase. RnhC in pathogenic mycobacteria is a possible candidate drug discovery target for tuberculosis and leprosy | Mycolicibacterium smegmatis |
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