Extended Data Fig. 1: PHAX phosphorylation analysis.
From: Structural basis for the synergistic assembly of the snRNA export complex
Masses of CK2-treated FL PHAX and PHAX41–80 were assessed using mass spectrometry (MS). a. FL PHAX was analyzed by LC-ESI-MS (liquid chromatography-electrospray). Data are presented after deconvolution of m/z (mass-to-charge ratio) to masses (expressed in Da). Spectra of FL PHAX before and after phosphorylation were compared. The full-length protein has between 3 and 5 phosphorylated sites (3 P, 4 P and 5 P). LC-ESI-MS data were collected using Mass hunter (v. 11.0, Agilent Technologies) and processed using Bioconfirm (v. 12.01, Agilent Technologies) and GPMAW (v. 7.00b2, Lighthouse Data, Denmark) software. b. PHAX (41–80) was analyzed by MALDI-MS (Matrix Assisted Laser Desorption Ionisation-mass spectrometry). MALDI-MS determines m/z values of singly charged PHAX41–80 ions. The m/z difference between the untreated PHAX (41–80) and the phosphorylated one indicates that PHAX41–80 carries 3 phosphorylated sites (3 P). An additional site (4 P) may be present. Peaks that are not labeled are due to adducts with non-volatile molecules (such as Na). MALDI-MS data were collected using flexControl™ (v.3.4, Bruker Daltonik) and processed using flexAnalysis™ (v. 3.4, Bruker Daltonik).
