(a) Immunoprecipitation using antihydroxyproline antibody
(HydroxyP) from 293FT cells that were transiently transfected with plasmids
encoding Flag-TFAM and HA-EGLN1, HA-EGLN2 and HA-EGLN3. Immunoblots show
co-immunoprecipitation of Flag-TFAM. n = 3 biological independent
experiments. (b-c) Mass spectrometry of unmodified biotinylated
TFAM-peptide-30-70. Shown is the representative fragmentation peptide
spectra of non-hydroxylated Biotin-KPVSSYLR (b) and non-hydroxylated
Biotin-EQLPIFKA (c). (d,e) Extracted ion chromatogram of biotinylated
unmodified and mono hydroxylated proline residues 53 (d) or proline residues
66 (e) TFAM peptide following an in vitro hydroxylation reaction with EglN3
with indicated concentration of ϒ-ketoglutarate (KG). Control
indicates unmodified biotinylated TFAM-peptide that was not subjected to
EGLN3 hydroxylation. (f) Hydroxylation levels of proline residues 53 and 66
of TFAM peptide following hydroxylation with EGLN3 generated via IVT with
indicated concentration of KG. Data are presented as mean values ±
SD. n = 3 biological experiments. One way ANOVA Tukey's Multiple
Comparison Test. *p <0.05, **p <0.01. p=0.0288, p=0.0143,
p=0.0148, p=0.0082. (g) Schematic illustration of synthetic biotinylated
TFAM peptide hydroxylated at P-OH-53 and P-OH-66 and naïve TFAM
peptide. (h) Autoradiograms showing recovery of 35S-labeled VHL protein (WT)
or corresponding disease mutants (as indicated) bound to biotinylated
HIF1α peptide (residues 556 to 575) with hydroxylated proline 564
(HIF1α-P-OH) and HIF2α peptide (residues 521 to 543) with
hydroxylated proline 531 (HIF2α-P-OH). Biotinylated HIF1α and
HIF2α naïve peptides were used as negative controls. n = 3
biological independent experiments. (i) Peptide pulldown using biotinylated
TFAM-P-OH-53/66 peptide incubated with whole-cell lysates from A498 cells
expressing HA-VHL WT or empty control. Biotinylated TFAM naïve
peptide was used as negative control. n = 3 biological independent
experiments.