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Literature summary for 4.6.1.24 extracted from
- Barnase and binase: twins with distinct fates (2011), FEBS J., 278, 3633-3643.
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | acquisition of male, female or bisexual sterility by transgenic plants with the help of barnase. The enzyme is useful in medical research, overview | Bacillus amyloliquefaciens |
| additional information | the enzyme is useful in medical research, overview | Bacillus pumilus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| genetic organization, low level expression of barnase by recombinant Bacillus subtilis strains bearing phoPR-null mutations | Bacillus amyloliquefaciens |
| genetic organization, production of binase by recombinant Bacillus subtilis strains bearing phoPR-null mutations is impossible | Bacillus pumilus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| barstar | a small protein of 89 amino acids, specifically inhibits barnase, barnase and barstar form a noncovalent one-to-one complex. Barstar inhibits barnase activity by sterically blocking its active site with an alpha-helix and adjacent loop. The association is stabilized by charge interaction involving the positively charged amino acid residues Lys27, Arg59, Arg83 and Arg87 of barnase and the negatively charged Asp35, Asp39 and Glu76 of barstar | Bacillus amyloliquefaciens | |
| additional information | no effective inhibition of barnase by RNase inhibitor YrdF | Bacillus amyloliquefaciens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted | Bacillus amyloliquefaciens | - |
- |
| extracellular | the enzyme is secreted | Bacillus pumilus | - |
- |
| additional information | 99% of binase is present outside of the cell and only below 1% is localized intracellularly | Bacillus pumilus | - |
- |
| additional information | about 3040% of barnase can be stored inside the cells for up to 90 min in complex with inhibitor barstar | Bacillus amyloliquefaciens | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 12213 | - |
1 * 12213, sequence calculation | Bacillus pumilus |
| 12382 | - |
1 * 12382, sequence calculation | Bacillus amyloliquefaciens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Bacillus amyloliquefaciens | barnase catalyses the overall hydrolysis of single-stranded RNA preferentially at guanylyl residues, yielding new guanosine 3'-phosphate and 5'-OH ends, in a two-step process with cleavage of the RNA chain by transesterification of a 5'-phosphoester bond to form a guanosine 2',3'-cyclic phosphate terminus in the first step, followed by its hydrolysis to a 3'-phosphate product in the second independent step | ? | - |
? |  |
| additional information | Bacillus pumilus | binase catalyses the overall hydrolysis of single-stranded RNA preferentially at guanylyl residues, yielding new guanosine 3'-phosphate and 5'-OH ends, in a two-step process with cleavage of the RNA chain by transesterification of a 5'-phosphoester bond to form a guanosine 2',3'-cyclic phosphate terminus in the first step, followed by its hydrolysis to a 3'-phosphate product in the second independent step | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus amyloliquefaciens | - |
- |
- |
| Bacillus pumilus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | binase is not produced by Bacillus pumilus when bacteria are grown on medium containing an inorganic source of nitrogen. Expression of binase is possible only in Spo0A-OFF cells | Bacillus pumilus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | barnase catalyses the overall hydrolysis of single-stranded RNA preferentially at guanylyl residues, yielding new guanosine 3'-phosphate and 5'-OH ends, in a two-step process with cleavage of the RNA chain by transesterification of a 5'-phosphoester bond to form a guanosine 2',3'-cyclic phosphate terminus in the first step, followed by its hydrolysis to a 3'-phosphate product in the second independent step | Bacillus amyloliquefaciens | ? | - |
? | |
| additional information | binase catalyses the overall hydrolysis of single-stranded RNA preferentially at guanylyl residues, yielding new guanosine 3'-phosphate and 5'-OH ends, in a two-step process with cleavage of the RNA chain by transesterification of a 5'-phosphoester bond to form a guanosine 2',3'-cyclic phosphate terminus in the first step, followed by its hydrolysis to a 3'-phosphate product in the second independent step | Bacillus pumilus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 12213, sequence calculation | Bacillus pumilus |
| monomer | 1 * 12382, sequence calculation | Bacillus amyloliquefaciens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| barnase | - |
Bacillus amyloliquefaciens |
| Binase | - |
Bacillus pumilus |
| guanyl-preferring RNase | - |
Bacillus pumilus |
| More | the enzyme belongs to the superfamily of microbial N1/T1 RNases | Bacillus amyloliquefaciens |
| More | the enzyme belongs to the superfamily of microbial N1/T1 RNases | Bacillus pumilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Bacillus amyloliquefaciens |
| 37 | - |
- |
Bacillus pumilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
- |
Bacillus amyloliquefaciens |
| 8.5 | - |
- |
Bacillus pumilus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 9 | stable | Bacillus pumilus |
| 3 | 9 | stbale | Bacillus amyloliquefaciens |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Bacillus amyloliquefaciens | - |
- |
9.2 |
| Bacillus pumilus | - |
- |
9.5 |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Bacillus pumilus | low concentrations of extracellular inorganic phosphate induce the expression of the binase gene | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | binase is involved in phosphate metabolism, low concentrations of extracellular inorganic phosphate induce the expression of phosphate regulon, Pho, genes, as well as the binase gene, binase expression is strongly dependent on a functional PhoP-PhoR two-component system | Bacillus pumilus |
| additional information | comparison with barnase from Bacillus amyloliquefaciens, overview. Mutation in resD leads to a significant decrease in binase production, whereas mutation in spo0A causes its hyperproduction. Expression of binase is possible only in Spo0A-OFF cells | Bacillus pumilus |
| additional information | comparison with binase from Bacillus pumilus, overview. Barnase expression is strictly dependent on activating Spo0A, the Spo0A protein is a multifunctional regulator that controls stress-related processes, such as sporulation, biofilm formation and cannibalism | Bacillus amyloliquefaciens |
| physiological function | barnase can help the population to win the competition with other bacteria for ecological niches, acting as a toxin. Toxic extracellular RNases and antitoxic barstar build an analogous system | Bacillus amyloliquefaciens |
| physiological function | binase can help the population to win the competition with other bacteria for ecological niches, acting as a toxin | Bacillus pumilus |
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