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  Mechanism of ribosome rescue by alternative ribosome-rescue factor B

Chan, K.-H., Petrychenko, V., Mueller, C., Maracci, C., Holtkamp, W., Wilson, D. N., et al. (2020). Mechanism of ribosome rescue by alternative ribosome-rescue factor B. Nature Communications, 11: 4106. doi:10.1038/s41467-020-17853-7.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0007-2B70-B Version Permalink: http://hdl.handle.net/21.11116/0000-0007-2C12-4
Genre: Journal Article

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 Creators:
Chan, K.-H.1, Author              
Petrychenko, V.2, Author              
Mueller, Claudia, Author
Maracci, C.1, Author              
Holtkamp, W.3, Author              
Wilson, Daniel N., Author
Fischer, N.2, Author              
Rodnina, M. V.3, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578598              
2Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              
3Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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Free keywords: Cryoelectron microscopy; Kinetics; Ribosome
 Abstract: Alternative ribosome-rescue factor B (ArfB) rescues ribosomes stalled on non-stop mRNAs by releasing the nascent polypeptide from the peptidyl-tRNA. By rapid kinetics we show that ArfB selects ribosomes stalled on short truncated mRNAs, rather than on longer mRNAs mimicking pausing on rare codon clusters. In combination with cryo-electron microscopy we dissect the multistep rescue pathway of ArfB, which first binds to ribosomes very rapidly regardless of the mRNA length. The selectivity for shorter mRNAs arises from the subsequent slow engagement step, as it requires longer mRNA to shift to enable ArfB binding. Engagement results in specific interactions of the ArfB C-terminal domain with the mRNA entry channel, which activates peptidyl-tRNA hydrolysis by the N-terminal domain. These data reveal how protein dynamics translate into specificity of substrate recognition and provide insights into the action of a putative rescue factor in mitochondria.

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Language(s): eng - English
 Dates: 2020-08-14
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-020-17853-7
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Title: Nature Communications
Source Genre: Journal
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Pages: 11 Volume / Issue: 11 Sequence Number: 4106 Start / End Page: - Identifier: -