Application | Comment | Organism |
---|---|---|
analysis | the absence of cysteine residues in MtTOP1 makes it an attractive system for introduction of potentially informative chemical or spectroscopic probes at specific positions via cysteine mutagenesis. Such probes could be useful for development of high throughput screening assays and can be utilized for fluorescence probe incorporation and fluorescence resonance energy transfer measurement with fluorophore-labeled oligonucleotide substrate | Mycobacterium tuberculosis |
Cloned (Comment) | Organism |
---|---|
plasmid-encoded recombinant MtTOP1 can complement the temperature sensitive topA function of Escherichia coli strain AS17 for growth at 42°C. The relaxation activity of recombinant wild-type MtTOP1 is functional in Escherichia coli. No complementation from the Y342A or G116S MtTOP1 mutants, but by mutant H139C, L170C, Y174C, T142C, and K524C. Overexpression of MtTOP1 mutant G116S leads to accumulation of cleavage complex formed by MtTOP1 in Escherichia coli | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
D111N | site-directed mutagenesis, the mutation is lethal for the host | Mycobacterium tuberculosis |
G116S | site-directed mutagenesis, MtTOP1 TOPRIM motif mutation, the mutation inhibits DNA religation. The DNA cleavage activity of MtTOP1-G116 S is Mg2+-dependent | Mycobacterium tuberculosis |
H139C | site-directed mutagenesis, the mutant can be labeled with fluorophores with no significant loss of relaxation activity, the mutant complements the temperature sensitive topA function of Escherichia coli strain AS17 | Mycobacterium tuberculosis |
K524C | site-directed mutagenesis, the mutant can be labeled with fluorophores with no significant loss of relaxation activity, the mutant complements the temperature sensitive topA function of Escherichia coli strain AS17 | Mycobacterium tuberculosis |
L170C | site-directed mutagenesis, the mutant can be labeled with fluorophores with no significant loss of relaxation activity, the mutant complements the temperature sensitive topA function of Escherichia coli strain AS17 | Mycobacterium tuberculosis |
T142C | site-directed mutagenesis, the mutant can be labeled with fluorophores with no significant loss of relaxation activity, the mutant complements the temperature sensitive topA function of Escherichia coli strain AS17 | Mycobacterium tuberculosis |
Y174C | site-directed mutagenesis, the mutant can be labeled with fluorophores with no significant loss of relaxation activity, the mutant complements the temperature sensitive topA function of Escherichia coli strain AS17 | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the DNA cleavage activity of MtTOP1-G116 S is Mg2+-dependent | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | structure-function analysis of MtTOP1, overview | Mycobacterium tuberculosis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structure-function analysis of MtTOP1, overview | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
MtTOP1 | - |
Mycobacterium tuberculosis |
Topoisomerase I | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
malfunction | accumulation of cleavage complex formed by inactivated MtTOP1 is lethal for the cell | Mycobacterium tuberculosis |
additional information | the TOPRIM motif DxDxxG is strictly conserved in type IA topoisomerase sequences and plays an essential role for divalent ion coordination and cleavage-religation of DNA during catalysis | Mycobacterium tuberculosis |