期刊
NATURE
卷 603, 期 7901, 页码 503-+出版社
NATURE PORTFOLIO
DOI: 10.1038/s41586-022-04416-7
关键词
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资金
- NIH [GM136960]
- Intramural Research Program of the National Library of Medicine at the NIH
- German Research Council [TRR174]
- DFG fellowship through the Graduate School of Quantitative Bioscience Munich (QBM)
A new rescue factor, SmrB, with endonuclease activity has been discovered. It cleaves mRNAs upstream of stalled ribosomes, allowing the ribosome rescue factor tmRNA to rescue upstream ribosomes.
Ribosome rescue pathways recycle stalled ribosomes and target problematic mRNAs and aborted proteins for degradation(1,2). In bacteria, it remains unclear how rescue pathways distinguish ribosomes stalled in the middle of a transcript from actively translating ribosomes(3-6). Here, using a genetic screen in Escherichia coli, we discovered a new rescue factor that has endonuclease activity. SmrB cleaves mRNAs upstream of stalled ribosomes, allowing the ribosome rescue factor tmRNA (which acts on truncated mRNAs(3)) to rescue upstream ribosomes. SmrB is recruited to ribosomes and is activated by collisions. Cryo-electron microscopy structures of collided disomes from E. coli and Bacillus subtilis show distinct and conserved arrangements of individual ribosomes and the composite SmrB-binding site. These findings reveal the underlying mechanisms by which ribosome collisions trigger ribosome rescue in bacteria.
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