Fig. 3: SFPQ interacts with the histone H3.3 chaperone DAXX.
From: SFPQ directs histone H3.3 deposition to R-loops in DNA repeats to protect genome stability
A Anti-SFPQ immunoprecipitation of ectopically expressed myc-tagged SFPQ followed by SDS-PAGE, Coomassie staining and identification of interacting proteins by MALDI-TOF mass spectrometry. B Immunoprecipitation of overexpressed myc-tagged SFPQ in H1299 cells. C Immunoprecipitation of overexpressed HA-DAXX in H1299 cells. D Co-immunoprecipitation of endogenous SFPQ and DAXX proteins in U-2 OS cells using specific antibodies. L.E., low exposure. E Combined immunofluorescence using anti-DAXX and anti-TRF2 antibodies in U-2 OS cells transfected with indicated siRNAs. Right panel, quantification of DAXX-TRF2 co-localization events. F Representative images of combined immunofluorescence with anti-DAXX and anti-CREST (centromere) antibodies in U-2 OS cells transfected with indicated siRNAs. Right panel, quantification of DAXX-CREST colocalization events. A–D representative images are shown. For quantifications, data represents the mean, error bars indicate standard deviation. N = number of independent experiments. n = number of analyzed nuclei. Arrowheads and zoomed images indicate co-localization events. An unpaired, two-sided Student’s t test was used to calculate statistical significance; p values are shown. Scale bar (1 μm) applies to all images in respective immunofluorescence panels. DNA was stained using DAPI (4’,6-diamidino-2-phenylindole). Source data are provided with this paper.
