Caenorhabditis elegans ddx-15 helicase fails to complement loss of Prp43p in Saccharomyces cerevisiae
Jonathan E Karpel

TL;DR
This study shows that a helicase protein from C. elegans cannot replace a similar protein in yeast, suggesting functional differences despite conservation.
Contribution
The novel finding is that DDX-15 from C. elegans fails to functionally complement Prp43p in yeast.
Findings
DDX-15 from C. elegans cannot rescue the loss of Prp43p in yeast.
Transcriptional repression experiments confirmed the functional incompatibility between DDX-15 and Prp43p.
Abstract
Helicase proteins have important roles in many aspects of RNA metabolism in the cell. The function of these highly conserved proteins is commonly preserved between organisms, yet in a few cases these homologues are found to have slightly different biochemical functions. Prp43 is a protein with varied roles in yeast, but here we show that the C. elegans homologue of this protein is unable to rescue the loss of Prp43p. By employing a transcriptional repression experiment, the expression of DDX-15 protein in yeast is not enough to complement the loss of Prp43p, which is a yeast essential protein.
Genes, proteins, chemicals, diseases, species, mutations and cell lines named across the full text — each resolved to its canonical identifier and authoritative record.
Click any figure to enlarge with its caption.
Figure 1Peer Reviews
No public reviews on file for this paper yet. If you reviewed it on a platform where reviews are public (OpenReview, ICLR, NeurIPS, ICML), you can paste yours below so the community can read it here.
Videos
No videos yet. Explain this paper in a talk, walkthrough, or lecture? Add one.
Taxonomy
TopicsRNA Research and Splicing · Genomics and Chromatin Dynamics · RNA modifications and cancer
