# The protein-protein interaction between two spliced leader trans -splicing factors is mediated by two interlinked α-helical domains

## TL;DR

This paper studies how two proteins, SNA-1 and SNA-2, interact in a worm species to help process RNA.

## Contribution

The study reveals that SNA-1 and SNA-2 interact via two interlinked alpha-helical domains.

## Key findings

- AlphaFold-Multimer predicts that the central region of SNA-1 and the C-terminal region of SNA-2 interlink.
- Yeast 2-hybrid assays confirm these regions are required and sufficient for the interaction.

## Abstract

SNA-1
and
SNA-2
proteins are involved in spliced leader
trans
-splicing in

Caenorhabditis elegans

. They are components of the SL1 snRNP that donates the spliced leader 1 RNA which replaces the 5' end of most pre-mRNAs.
SNA-1
and
SNA-2
bind to each other, but the nature of their interaction is unclear. AlphaFold-Multimer predicts that the central region of
SNA-1
and the C-terminal region of
SNA-2
, each consisting of 3 α-helices, interlink to bring about the interaction between these proteins. Using yeast 2-hybrid assays we demonstrate that these regions are required and sufficient for this unusual mode of interaction between two proteins.