# Caenorhabditis elegans ddx-15 helicase fails to complement loss of Prp43p in Saccharomyces cerevisiae

**Authors:** Jonathan E Karpel

PMC · DOI: 10.17912/micropub.biology.001113 · 2024-01-22

## 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.

## Key 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.

## Linked entities

- **Genes:** DHX15 (DEAH-box helicase 15) [NCBI Gene 1665]
- **Proteins:** DHX15 (DEAH-box helicase 15)
- **Species:** Caenorhabditis elegans (taxon 6239), Saccharomyces cerevisiae (taxon 4932)

## Full-text entities

- **Genes:** PRP43 (DEAH-box ATP-dependent RNA helicase PRP43) [NCBI Gene 852757]
- **Species:** Saccharomyces cerevisiae (baker's yeast, species) [taxon 4932], C. elegans [taxon 328850]

## Figures

1 figure with captions in the complete paper: https://tomesphere.com/paper/PMC10853815/full.md

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Source: https://tomesphere.com/paper/PMC10853815