Fig. 5: KDM4E catalyses Arg-20 hydroxylation of recombinant histone H2a and calf thymus histone H2a. | Communications Biology

Fig. 5: KDM4E catalyses Arg-20 hydroxylation of recombinant histone H2a and calf thymus histone H2a.

From: JmjC catalysed histone H2a N-methyl arginine demethylation and C4-arginine hydroxylation reveals importance of sequence-reactivity relationships

Fig. 5

a Representative deconvoluted LC–MS analysis of KDM4E-treated calf histone H2a (red) showing a +16 Da mass shift corresponding to addition of a hydroxyl group and −28 Da mass shifts corresponding to demethylation. Three independent assay repeats were carried out. ‘No enzyme control’ spectrum in black, ‘KDM4E-treated sample spectrum in red. b LC–MS/MS analysis of KDM4E-treated calf histone H2a. No evidence for hydroxylation was detected in the S(+27.99)SRAGLQFPVGR (−10logP: 50.3) fragment from the starting material (See Supplementary Fig. 15a) while evidence for hydroxylation at R20 was observed in the corresponding fragment with KDM4E treatment, i.e. (−10logP: 32.2) S(+27.99)SR(+16.00)AGLQFPVGR. See Supplementary Fig. 15b,c for ion tables. The +28 Da mass shift on the N-terminal Ser is due to N-formylation caused by formic acid used to quench the tryptic digestion.

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