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  Ribosome-bound Get4/5 facilitates the capture of tail-anchored proteins by Sgt2 in yeast

Zhang, Y., Laurentiis, E. D., Bohnsack, K. E., Wahlig, M., Ranjan, N., Gruseck, S., et al. (2021). Ribosome-bound Get4/5 facilitates the capture of tail-anchored proteins by Sgt2 in yeast. Nature Communications, 12: 782. doi:10.1038/s41467-021-20981-3.

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 Creators:
Zhang, Y., Author
Laurentiis, E. De, Author
Bohnsack, K. E., Author
Wahlig, M., Author
Ranjan, N.1, Author              
Gruseck, S., Author
Hackert, P., Author
Wölfle, T., Author
Rodnina, M. V.2, Author              
Schwappach, B.3, Author              
Rospert, S., Author
Affiliations:
1Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578598              
2Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
3Max Planck Fellow Blanche Schwappach, ou_1548137              

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Free keywords: Chaperones; Membrane proteins; Ribosomal proteins
 Abstract: The guided entry of tail-anchored proteins (GET) pathway assists in the posttranslational delivery of tail-anchored proteins, containing a single C-terminal transmembrane domain, to the ER. Here we uncover how the yeast GET pathway component Get4/5 facilitates capture of tail-anchored proteins by Sgt2, which interacts with tail-anchors and hands them over to the targeting component Get3. Get4/5 binds directly and with high affinity to ribosomes, positions Sgt2 close to the ribosomal tunnel exit, and facilitates the capture of tail-anchored proteins by Sgt2. The contact sites of Get4/5 on the ribosome overlap with those of SRP, the factor mediating cotranslational ER-targeting. Exposure of internal transmembrane domains at the tunnel exit induces high-affinity ribosome binding of SRP, which in turn prevents ribosome binding of Get4/5. In this way, the position of a transmembrane domain within nascent ER-targeted proteins mediates partitioning into either the GET or SRP pathway directly at the ribosomal tunnel exit.

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Language(s): eng - English
 Dates: 2021-02-04
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-20981-3
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Title: Nature Communications
Source Genre: Journal
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Pages: 17 Volume / Issue: 12 Sequence Number: 782 Start / End Page: - Identifier: -