# An Hsp70 Chaperone Is Involved in Meiotic Silencing by Unpaired DNA

## TL;DR

This paper shows that an Hsp70 chaperone helps silence unpaired genes during meiosis in a fungus by interacting with an Argonaute protein.

## Contribution

The study identifies a role for Hsp70 in meiotic silencing by unpaired DNA in Neurospora crassa.

## Key findings

- An Hsp70 protein interacts with the SMS-2 Argonaute in Neurospora.
- Hsp70 mediates the silencing of unpaired genes during meiosis.
- This mechanism resembles the Hsp70 role in Argonaute activation in Drosophila.

## Abstract

In the filamentous fungus Neurospora crassa, a gene not having a pairing partner during meiosis is seen as a potential intruder and is targeted by a mechanism called meiotic silencing by unpaired DNA (MSUD). MSUD employs core RNA interference (RNAi) components such as the SMS-2 Argonaute, which uses small interfering RNAs (siRNAs) as guides to seek out mRNAs from unpaired genes for silencing. In Drosophila melanogaster, the heat shock protein 70 (Hsp70) chaperone system facilitates the conformational activation of an Argonaute and allows it to load siRNAs. Here, our results demonstrate that an Hsp70 protein in Neurospora interacts with SMS-2 and mediates the silencing of unpaired genes.