PT  - JOURNAL ARTICLE
AU  - Adrien Birot
AU  - Krzysztof Kus
AU  - Emily Priest
AU  - Ahmad Al Alwash
AU  - Alfredo Castello
AU  - Shabaz Mohammed
AU  - Lidia Vasiljeva
AU  - Cornelia Kilchert
TI  - RNA-binding protein Mub1 and the nuclear RNA exosome act to fine-tune environmental stress response
AID  - 10.26508/lsa.202101111
DP  - 2022 Feb 01
TA  - Life Science Alliance
PG  - e202101111
VI  - 5
IP  - 2
4099  - https://www.life-science-alliance.org/content/5/2/e202101111.short
4100  - https://www.life-science-alliance.org/content/5/2/e202101111.full
SO  - Life Sci. Alliance2022 Feb 01; 5
AB  - The nuclear RNA exosome plays a key role in controlling the levels of multiple protein-coding and non-coding RNAs. Recruitment of the exosome to specific RNA substrates is mediated by RNA-binding co-factors. The transient interaction between co-factors and the exosome as well as the rapid decay of RNA substrates make identification of exosome co-factors challenging. Here, we use comparative poly(A)+ RNA interactome capture in fission yeast expressing three different mutants of the exosome to identify proteins that interact with poly(A)+ RNA in an exosome-dependent manner. Our analyses identify multiple RNA-binding proteins whose association with RNA is altered in exosome mutants, including the zinc-finger protein Mub1. Mub1 is required to maintain the levels of a subset of exosome RNA substrates including mRNAs encoding for stress-responsive proteins. Removal of the zinc-finger domain leads to loss of RNA suppression under non-stressed conditions, altered expression of heat shock genes in response to stress, and reduced growth at elevated temperature. These findings highlight the importance of exosome-dependent mRNA degradation in buffering gene expression networks to mediate cellular adaptation to stress.