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Chemical Compound Review

Permanganat     oxido-trioxo-manganese

Synonyms: Permanganate, Manganat(VII), MnO4-, AG-D-85735, CHEBI:25939, ...
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Disease relevance of oxido-trioxo-manganese


High impact information on oxido-trioxo-manganese

  • Thymines at symmetrical positions of the OBR within oriP were oxidized when cells were treated with permanganate, suggestive of bends or other distortions of DNA structure at these positions; binding of EBNA1 in vitro to total DNA from Raji cells induced reactivity to permanganate at identical positions [6].
  • In contrast, growth cones of nonadrenergic sensory neurons dissociated from dorsal root ganglia and fixed with permanganate lacked SGV and possessed small clear vesicles [7].
  • The permanganate data also provided evidence that Pol II encountered different rate-limiting steps, following initiation in the presence of Tet(on)-HSF and Tet(on)-VP16(A2) [8].
  • Using permanganate genomic footprinting, we observed that various levels of Gal4p induction resulted in an even distribution of RNA polymerase throughout the first 76 nucleotides of the transcribed region [9].
  • Permanganate treatment of intact salivary glands was used to further characterize each promoter construct [10].

Chemical compound and disease context of oxido-trioxo-manganese


Biological context of oxido-trioxo-manganese

  • Active and inactive c-myc genes yielded different patterns of S1 nuclease and permanganate sensitivity, indicating alternative chromatin configurations of active and silent genes [13].
  • EBNA1 binds cooperatively to four recognition sites in the dyad symmetry (DS) element of oriP, causing alterations in the origin DNA structure, which can be detected by the increased sensitivity of one Thy residue in two of the binding sites to permanganate oxidation [1].
  • We have shown that the EBNA1 DNA binding and dimerization domains are sufficient to induce permanganate sensitivity and that amino acids 463-467, which form an extended chain that travels along the minor groove of the EBNA1 recognition site, play an important role in generating the DNA distortion [1].
  • To identify the reaction intermediates that form by the human excision repair nuclease, we adopted three approaches: purification of functional DNA.protein complexes, permanganate footprinting, and the employment as substrate of presumptive DNA reaction intermediates containing unwound sequences 5' to, 3' to, or encompassing the DNA lesion [14].
  • To better understand the significance of this EBNA1-induced origin distortion, we have investigated the DNA sequence and EBNA1 amino acid requirements for permanganate sensitivity [1].

Anatomical context of oxido-trioxo-manganese


Associations of oxido-trioxo-manganese with other chemical compounds


Gene context of oxido-trioxo-manganese

  • Whereas in the TDH2 promoter permanganate reactivity was entirely abolished, the reactivity at the GAL1 and GAL10 promoter regions was only moderately affected [24].
  • DNA unwinding was probed with an in vivo permanganate reactivity assay, in a temperature-sensitive mutant of RAD25 [24].
  • High resolution run-on analysis and in vivo permanganate-dependent footprinting showed that this holds true for the c-fos gene in unstimulated cells where a strong block to transcription elongation was evidenced [25].
  • Two thymines occur at unique positions within EBNA-1 binding sites 1 and 4 at the DS and become sensitive to oxidation by permanganate when EBNA-1 binds, but mutation of each to the consensus base, adenine, actually improved the activity of each half of the DS slightly [26].
  • In addition to the permanganate-sensitive distortion, the full-length RAP1, but not its DNA-binding domain, induces a bend in DNA 5' of the recognition sequence, altering the electrophoretic mobility of the protein-DNA complex [27].

Analytical, diagnostic and therapeutic context of oxido-trioxo-manganese

  • By mobility shift assay, permanganate reactivity and in vitro transcription experiments, we show that repression is much stronger with Esigma(70) than with Esigma(S) holoenzyme [28].
  • The TG formed was identified by ultraviolet light (340 nm) detection following separation on a reverse phase high performance liquid chromatography system and by fluorescent detection of the permanganate oxidation product separated on a strong anion-exchange system [29].
  • Silver-staining (native fast silver stain, ammoniacal silver stain, permanganate silver stain), Coomassie-staining (R-250, G-250), metal ion-reverse-staining (zinc, copper), and fluorescent chromophore-staining (SYPRO Ruby) methods were used to visualize the IgG oligomers [30].
  • The protein zones were then excised, separated by SDS-PAGE, and subunits visualized with a permanganate silver stain [30].
  • The variant forms of individual topoisomers were separated by agarose gel electrophoresis and their reactivities to permanganate and acid-induced depurination were compared [31].


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