IndraLab

Statements

PCMT1 methylates TP53. 11 / 11
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"To confirm that PIMT methylates p53 at isoaspartate residues 29 and 30, we synthesized peptides consisting of amino acids 22–40 of p53, in which asparagines 29 and 30 were replaced with isoaspartates (N29IsoD, N30IsoD and N29,30IsoD)."
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"We also find that PIMT methylates p53 at isoaspartate residues 29 and 30, which is required to negatively regulate the p53 activity."
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"PIMT methylated the p53 peptide during a 30-min incubation period and the level of methylated peptide increased with increasing incubation time ( xref )."
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"Next, we determined whether PIMT methylates p53 under physiological conditions through nano-LC-ESI-MS/MS analysis of endogenous p53 purified from U2OS cells or ectopic-expressed p53 purified from H1299 cells under conditions in which the PIMT-catalyzed methylation of the isoaspartyl residues was stable enough for detection ( xref )."
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"Because PIMT interacted with p53 and its methylase activity was necessary for regulating p53, we examined whether PIMT directly methylates p53."
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"Using an in vitro methylation assay, we found that PIMT methylated p53, whereas the PIMT G88A mutant did not (XREF_FIG and XREF_SUPPLEMENTARY)."
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"The N terminus of p53 (amino acids 1-82) was methylated by PIMT, but not by the PIMT G88A mutant (XREF_FIG)."
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"PIMT methylated the p53 peptide during a 30-min incubation period and the level of methylated peptide increased with increasing incubation time (XREF_FIG)."
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"Next, we determined whether PIMT methylates p53 under physiological conditions through nano-LC-ESI-MS/MS analysis of endogenous p53 purified from U2OS cells or ectopic expressed p53 purified from H1299 cells under conditions in which the PIMT catalyzed methylation of the isoaspartyl residues was stable enough for detection (XREF_FIG)."
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"We show that asparagine residues 29 and 30 of p53 are methylated by PIMT in vivo and in vitro ."
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"Because PIMT interacted with p53 and its methylase activity was necessary for regulating p53, we examined whether PIMT directly methylates p53."
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