EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.6 | recombinant Rpb2 R512C, TAP-tagged at the C-terminus of the RNAP II Rpb9 subunit | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.7.6 | E529A | the substitution mutant is are faster than the wild-type enzyme in RNA elongation | Saccharomyces cerevisiae |
2.7.7.6 | E529D | the substitution mutant is are faster than the wild-type enzyme in RNA elongation | Saccharomyces cerevisiae |
2.7.7.6 | E529Q | the substitution mutant is are slower than the wild-type enzyme in RNA elongation | Saccharomyces cerevisiae |
2.7.7.6 | additional information | simulation of diverse McJ25-resistant mutations and their effects on enzyme activity, overview | Thermus thermophilus |
2.7.7.6 | R428A | site-directed mutagenesis, designed based on substitutions at the homologous position (Rpb2 R512) of Saccharomyces cerevisiae RNAP II, used as a reference structure, molecular dynamics simulations with starting Tt RNAP TEC structure, PDB 205J, that is in a strained, catalytic conformation that responds very sensitively to the R428A substitution but is stable for wild-type enzyme, overview. Long range conformational coupling linking a dynamic segment of the bridge alpha-helix, the extended fork loop, the active site, and the trigger loop-trigger helix is apparent and adversely affected in beta R428A RNAP. The R428A substitution is instable in the i+1 dTMP-ATP base pair, as indicated by fluctuations in the dTMP O4-ATP N6 base pairing distance in R428A | Thermus thermophilus |
2.7.7.6 | R512C | site-directed mutagenesis, the highly conserved residue is located about 20 A from Mg2+-I and just C-terminal to the fork loop, molecular dynamics simulations, overview. Mutant Sc Rpb2 R512C is slow in elongation and shows transcriptional defects. Rpb2 R512C may have a defect in CTP-Mg2+ sequestration | Saccharomyces cerevisiae |
2.7.7.6 | R766A | the substitution is lethal, consistent with an important role for this invariant latch residue | Saccharomyces cerevisiae |
2.7.7.6 | R766Q | the substitution is lethal, consistent with an important role for this invariant latch residue | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.6 | alpha-Amanitin | the potent Sc RNAP II inhibitor binds to a ternary elongation complex with an open wedged conformation of the trigger loop | Saccharomyces cerevisiae | |
2.7.7.6 | Streptolydigin | the antibiotic binds to a Tt RNAP TEC with an open trigger loop | Thermus thermophilus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.6 | Mg2+ | required | Thermus thermophilus | |
2.7.7.6 | Mg2+ | required | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.6 | ATP + RNAn | Thermus thermophilus | - |
diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | ATP + RNAn | Saccharomyces cerevisiae | - |
diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | CTP + RNAn | Thermus thermophilus | - |
diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | CTP + RNAn | Saccharomyces cerevisiae | - |
diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | GTP + RNAn | Thermus thermophilus | - |
diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | GTP + RNAn | Saccharomyces cerevisiae | - |
diphosphate + RNAn+1 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.6 | Saccharomyces cerevisiae | - |
strains YZS84 and YDP19 | - |
2.7.7.6 | Thermus thermophilus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.6 | ATP + RNAn | - |
Thermus thermophilus | diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | ATP + RNAn | - |
Saccharomyces cerevisiae | diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | CTP + RNAn | - |
Thermus thermophilus | diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | CTP + RNAn | - |
Saccharomyces cerevisiae | diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | GTP + RNAn | - |
Thermus thermophilus | diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | GTP + RNAn | - |
Saccharomyces cerevisiae | diphosphate + RNAn+1 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.7.6 | multi-subunit RNA polymerase | - |
Thermus thermophilus |
2.7.7.6 | multi-subunit RNA polymerase | - |
Saccharomyces cerevisiae |
2.7.7.6 | RNAP | - |
Thermus thermophilus |
2.7.7.6 | RNAP II | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.7.6 | 25 | - |
assay at | Thermus thermophilus |
2.7.7.6 | 25 | - |
assay at | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.6 | 7.6 | - |
assay at | Thermus thermophilus |
2.7.7.6 | 7.6 | - |
assay at | Saccharomyces cerevisiae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.7.6 | malfunction | mutant Sc Rpb2 R512C is slow in elongation | Saccharomyces cerevisiae |
2.7.7.6 | malfunction | R428A RNAP is instable | Thermus thermophilus |
2.7.7.6 | additional information | in vitro assembly of Sc RNAP II ternary elongation complexes, overview. RNA polymerase in a catalytic conformation demonstrates that the active site dNMP-NTP base pair must be substantially dehydrated to support full active site closing and optimum conditions for phosphodiester bond synthesis. An active site latch assembly that includes a key trigger helix residue beta' H1242 and highly conserved active site residues beta E445 and R557 appears to help regulate active site hydration/dehydration. Molecular dynamics simulations, overview | Saccharomyces cerevisiae |
2.7.7.6 | additional information | modeling of Tt RNAP TEC containing a closed, catalytic trigger helix conformation. RNA polymerase in a catalytic conformation demonstrates that the active site dNMP-NTP base pair must be substantially dehydrated to support full active site closing and optimum conditions for phosphodiester bond synthesis. An active site latch assembly that includes a key trigger helix residue beta' H1242 and highly conserved active site residues beta E445 and R557 appears to help regulate active site hydration/dehydration. Molecular dynamics simulations, overview | Thermus thermophilus |