English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Ribosome-associated chloroplast SRP54 enables efficient co-translational membrane insertion of key photosynthetic proteins

Hristou, A., Gerlach, I., Stolle, D. S., Neumann, J., Bischoff, A., Dünschede, B., et al. (2019). Ribosome-associated chloroplast SRP54 enables efficient co-translational membrane insertion of key photosynthetic proteins. The Plant Cell, 31, 2734-2750. doi:10.1105/tpc.19.00169.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0005-103A-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-3F4E-F
Genre: Journal Article

Files

show Files

Locators

show
hide
Locator:
Link (Any fulltext)
Description:
-

Creators

show
hide
 Creators:
Hristou, Athina1, Author
Gerlach, I.2, Author              
Stolle, Dominique S1, Author
Neumann, Jennifer1, Author
Bischoff, Annika1, Author
Dünschede, Beatrix1, Author
Nowaczyk, Marc M1, Author
Zoschke, R.2, Author              
Schünemann, Danja1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Translational Regulation in Plants, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_2324691              

Content

show
hide
Free keywords: -
 Abstract: Key proteins of the photosynthetic complexes are encoded on the chloroplast genome and co-translationally inserted into the thylakoid membrane. However, the molecular details of this process are largely unknown. Here, we demonstrate by ribosome profiling that the conserved chloroplast signal recognition particle subunit, cpSRP54, is required for efficient co-translational targeting of several central photosynthetic proteins, like the photosystem II PsbA (D1) subunit. High-resolution analysis of membrane-associated and soluble ribosome footprints revealed that the SRP-dependent membrane targeting of PsbA is already initiated at a very early translation step before exposure of the nascent chain from the ribosome. Different to cytosolic SRP, which contacts the ribosome close to the peptide tunnel exit site, analysis of the cpSRP54/ribosome binding interface revealed a direct interaction of cpSRP54 and the ribosomal subunit uL4, which is not located at the tunnel exit site but forms a part of the internal peptide tunnel wall by a loop domain. The plastid specific C-terminal tail region of cpSRP54 plays a crucial role in uL4 binding. Our data indicate a novel mechanism of SRP-dependent membrane protein transport with the cpSRP54/uL4 interaction as a central element in early initiation of co-translational membrane targeting.

Details

show
hide
Language(s): eng - English
 Dates: 20192019
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1105/tpc.19.00169
BibTex Citekey: Hristoutpc.00169.2019
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Plant Cell
  Abbreviation : Plant C
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Rockville : American Society of Plant Physiologists
Pages: - Volume / Issue: 31 Sequence Number: - Start / End Page: 2734 - 2750 Identifier: ISSN: 1532-298X
CoNE: https://pure.mpg.de/cone/journals/resource/1532-298X