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  Translation termination depends on the sequential ribosomal entry of eRF1 and eRF3.

Beissel, C., Neumann, B., Uhse, S., Hampe, I., Karki, P., & Krebber, H. (2019). Translation termination depends on the sequential ribosomal entry of eRF1 and eRF3. Nucleic Acids Research, 47(9), 4798-4813. doi:10.1093/nar/gkz177.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0004-49CE-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0004-49D4-B
Genre: Journal Article

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Beissel , C., Author
Neumann, B., Author
Uhse, S., Author
Hampe , I., Author
Karki, P.1, Author              
Krebber, H., Author
Affiliations:
1Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578598              

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 Abstract: Translation termination requires eRF1 and eRF3 for polypeptide-and tRNA-release on stop codons. Additionally, Dbp5/DDX19 and Rli1/ABCE1 are required; however, their function in this process is currently unknown. Using a combination of in vivo and in vitro experiments, we show that they regulate a stepwise assembly of the termination complex. Rli1 and eRF3-GDP associate with the ribosome first. Subsequently, Dbp5-ATP delivers eRF1 to the stop codon and in this way prevents a premature access of eRF3. Dbp5 dissociates upon placing eRF1 through ATP-hydrolysis. This in turn enables eRF1 to contact eRF3, as the binding of Dbp5 and eRF3 to eRF1 is mutually exclusive. Defects in the Dbp5-guided eRF1 delivery lead to premature contact and premature dissociation of eRF1 and eRF3 from the ribosome and to subsequent stop codon readthrough. Thus, the stepwise Dbp5-controlled termination complex assembly is essential for regular translation termination events. Our data furthermore suggest a possible role of Dbp5/DDX19 in alternative translation termination events, such as during stress response or in developmental processes, which classifies the helicase as a potential drug target for nonsense suppression therapy to treat cancer and neurodegenerative diseases.

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Language(s): eng - English
 Dates: 2019-05-152019-05-21
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1093/nar/gkz177
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Title: Nucleic Acids Research
Source Genre: Journal
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Pages: - Volume / Issue: 47 (9) Sequence Number: - Start / End Page: 4798 - 4813 Identifier: -