한빛사논문
- 조회418
Esther N Park 1, Timur Mackens-Kiani 2, Rebekah Berhane 1, Hanna Esser 2, Chimeg Erdenebat 2, A Maxwell Burroughs 3, Otto Berninghausen 2, L Aravind 3, Roland Beckmann 2, Rachel Green 1,4 & Allen R Buskirk 1,*
1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
2Gene Center and Department of Biochemistry, University ofMunich, Munich, Germany.
3Computational Biology Branch, Intramural Research Program, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA.
4Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA
*Corresponding author: correspondence to Allen R Buskirk
Abstract
Stalled ribosomes are rescued by pathways that recycle the ribosome and target the nascent polypeptide for degradation. In E. coli, these pathways are triggered by ribosome collisions through the recruitment of SmrB, a nuclease that cleaves the mRNA. In B. subtilis, the related protein MutS2 was recently implicated in ribosome rescue. Here we show that MutS2 is recruited to collisions by its SMR and KOW domains, and we reveal the interaction of these domains with collided ribosomes by cryo-EM. Using a combination of in vivo and in vitro approaches, we show that MutS2 uses its ABC ATPase activity to split ribosomes, targeting the nascent peptide for degradation through the ribosome quality control pathway. However, unlike SmrB, which cleaves mRNA in E. coli, we see no evidence that MutS2 mediates mRNA cleavage or promotes ribosome rescue by tmRNA. These findings clarify the biochemical and cellular roles of MutS2 in ribosome rescue in B. subtilis and raise questions about how these pathways function differently in diverse bacteria.
논문정보
- Research article
- 2023년 12월 (BRIC 등록일 2023-12-19)
- 국외 연구진
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