Fig. 1
From: Dbl2 interacts with helicases and an endonuclease to maintain the integrity of repetitive regions

Dbl2 is associated with DNA repair proteins. (A) List of selected proteins with determined label-free quantification (LFQ) intensities (see Material and Methods) co-purified with Dbl2-TAP. Proteins associated with Dbl2 were isolated from cycling S. pombe cells (strain SP1210) by tandem affinity purification and analyzed by mass spectrometry. Results of three independent experiments are shown (Dbl2_S1, Dbl2_S2, Dbl2_S3). Proteins of higher abundance are indicated by red color, while proteins of lower abundance are indicated by green color. For a complete list of co-purified proteins and their post-translational modifications, see Table S4. (B, C, D) S. cerevisiae strains (SP1, Table S1) expressing Dbl2 fused to the GAL4 transcription activation domain (AD) and Fml1, Mhf1, Mus81, Rmi1, or Dbl2 fused to the GAL4 DNA-binding domain (BD) were grown on SD plates lacking Leu and Trp (SD-LW) and then spotted at tenfold serial dilutions on SD-LW or SD plates lacking Leu, Trp, and His (SD-LWH) or SD plates lacking Leu, Trp, and Ade (SD-LWA). The empty vectors pGADT7 and pGBKT7 containing AD and BD, respectively, were used as negative controls. Growth on plates without His or Ade indicates interaction between the fusion proteins. In cases where the strains did not grow on plates without Ade, those plates are not shown.