Limited Portability of G-Patch Domains in Regulators of the Prp43 RNA Helicase Required for Pre-mRNA Splicing and Ribosomal RNA Maturation in Saccharomyces cerevisiae

Files in this data supplement:

  • Supporting Information: Figures S1-S11 and References (PDF, 1 MB)
  • Figure S1: Oligonucleotide list. (PDF, 114 KB)
  • Figure S2: The Y2H G-patch peptides are stable in yeast. (PDF, 153 KB)
  • Figure S3: The Sqs1 G-patch partially supports Spp382 function. (PDF, 1 MB)
  • Figure S4: Multiple sequence alignment of G-patch domains. (PDF, 98 KB)
  • Figure S5: Spp382 is largely insensitive to G-patch P90 mutation. (PDF, 141 KB)
  • Figure S6: G-patch peptides show differential binding to full length Prp43 protein. (PDF, 140 KB)
  • Figure S7: The Spp382-Pxr1 G-patch substitution derivatives are equivalently expressed. (PDF, 133 KB)
  • Figure S8: The primary Prp43 binding site within Pxr1 lies downstream of the G-patch. (PDF, 155 KB)
  • Figure S9: Most PXR1 deletion derivatives produce stable proteins. (PDF, 156 KB)
  • Figure S10: Most PRP43 deletion derivatives are well expressed in yeast. (PDF, 139 KB)
  • Figure S11: Most isolated Prp43 domains are stable in yeast. (PDF, 136 KB)