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Literature summary for 5.6.2.1 extracted from

  • Huang, F.; He, Z.G.
    Characterization of an interplay between a Mycobacterium tuberculosis MazF homolog, Rv1495 and its sole DNA topoisomerase I (2010), Nucleic Acids Res., 38, 8219-8230.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged TopA in Escherichia coli strain BL21 Mycolicibacterium smegmatis
expression of His-tagged TopA in Escherichia coli strain BL21 Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
Rv1495 inhibits the DNA cleavage activity of MtbTopA as well as its function of relaxation of supercoiled DNA. An N-terminus fragment of Rv1495, designated Rv1495-N(29-56), lost mRNA cleavage activity, but retained a significant physical interaction and inhibitory effect on TopA proteins, overview. No DNA-binding activity is seen with Rv1495, even at a high protein concentration Mycobacterium tuberculosis
Rv1495 inhibits the DNA cleavage activity of MsTopA as well as its function of relaxation of supercoiled DNA. An N-terminus fragment of Rv1495, designated Rv1495-N(29-56), lost mRNA cleavage activity, but retained a significant physical interaction and inhibitory effect on TopA proteins in vitro and in vivo. MsmTopA associates with Rv1495 in vivo because an obvious and a specific hybridization signal is detected. No DNA-binding activity is seen with Rv1495, even at a high protein concentration Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mycolicibacterium smegmatis topoisomerase I shows a negative interplay between MazF protein Rv1495. Through its C-terminal domain, MsTopA physically interacts with and inhibits the mRNA cleavage activity of Rv1495. Rv1495, in turn, inhibits the DNA cleavage activity of MsTopA as well as its function of relaxation of supercoiled DNA ?
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 ?
additional information Mycobacterium tuberculosis topoisomerase I shows a negative interplay between MazF protein Rv1495. Through its C-terminal domain, MtbTopA physically interacts with and inhibits the mRNA cleavage activity of Rv1495, overview. Rv1495, in turn, inhibits the DNA cleavage activity of MtbTopA as well as its function of relaxation of supercoiled DNA ?
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 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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Mycolicibacterium smegmatis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information topoisomerase I shows a negative interplay between MazF protein Rv1495. Through its C-terminal domain, MsTopA physically interacts with and inhibits the mRNA cleavage activity of Rv1495. Rv1495, in turn, inhibits the DNA cleavage activity of MsTopA as well as its function of relaxation of supercoiled DNA Mycolicibacterium smegmatis ?
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 ?
additional information topoisomerase I shows a negative interplay between MazF protein Rv1495. Through its C-terminal domain, MtbTopA physically interacts with and inhibits the mRNA cleavage activity of Rv1495, overview. Rv1495, in turn, inhibits the DNA cleavage activity of MtbTopA as well as its function of relaxation of supercoiled DNA Mycobacterium tuberculosis ?
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 ?

Synonyms

Synonyms Comment Organism
DNA topoisomerase I
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 Mycolicibacterium smegmatis
DNA topoisomerase I
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 Mycobacterium tuberculosis
MsTopA
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 Mycolicibacterium smegmatis
MtbTopA
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 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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 assay at Mycolicibacterium smegmatis
37
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 assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Mycolicibacterium smegmatis
7.8
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 assay at Mycobacterium tuberculosis