Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway
Abstract
Thylakoids are complex sub-organellar membrane systems whose role in photosynthesis makes them critical to life. Thylakoids require the coordinated expression of both nuclear- and plastid-encoded proteins to allow rapid response to changing environmental conditions. Transport of cytoplasmically synthesized proteins to thylakoids or the thylakoid lumen is complex; the process involves transport across up to three membrane systems with routing through three aqueous compartments. Protein transport in thylakoids is accomplished by conserved ancestral prokaryotic plasma membrane translocases containing novel adaptations for the sub-organellar location. This review focuses on the evolutionarily conserved chloroplast twin arginine transport (cpTat) pathway. An overview is provided of known aspects of the cpTat components, energy requirements, and mechanisms with a focus on recent discoveries. Some of the most exciting new studies have been in determining the structural architecture of the membrane complex involved in forming the point of passage for the precursor and binding features of the translocase components. The cpTat system is of particular interest because it transports folded protein domains using only the proton motive force for energy. In summary, the implications for mechanism of translocation by recent studies focusing on interactions between membrane Tat components and with the translocating precursor will be discussed.
- Publication Date:
- Research Org.:
- Miami Univ., Oxford, OH (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division; National Institutes of Health (NIH)
- OSTI Identifier:
- 1830776
- Alternate Identifier(s):
- OSTI ID: 1593755
- Grant/Contract Number:
- SC0014441; P41-GM103311
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Photosynthesis Research
- Additional Journal Information:
- Journal Volume: 138; Journal Issue: 3; Journal ID: ISSN 0166-8595
- Publisher:
- Springer
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; twin arginine translocase; chloroplast; thylakoid; Chloroplast twin arginine transport; cpTat; Thylakoid protein routing
Citation Formats
New, Christopher Paul, Ma, Qianqian, and Dabney-Smith, Carole. Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway. United States: N. p., 2018.
Web. doi:10.1007/s11120-018-0567-z.
New, Christopher Paul, Ma, Qianqian, & Dabney-Smith, Carole. Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway. United States. https://doi.org/10.1007/s11120-018-0567-z
New, Christopher Paul, Ma, Qianqian, and Dabney-Smith, Carole. Sun .
"Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway". United States. https://doi.org/10.1007/s11120-018-0567-z. https://www.osti.gov/servlets/purl/1830776.
@article{osti_1830776,
title = {Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway},
author = {New, Christopher Paul and Ma, Qianqian and Dabney-Smith, Carole},
abstractNote = {Thylakoids are complex sub-organellar membrane systems whose role in photosynthesis makes them critical to life. Thylakoids require the coordinated expression of both nuclear- and plastid-encoded proteins to allow rapid response to changing environmental conditions. Transport of cytoplasmically synthesized proteins to thylakoids or the thylakoid lumen is complex; the process involves transport across up to three membrane systems with routing through three aqueous compartments. Protein transport in thylakoids is accomplished by conserved ancestral prokaryotic plasma membrane translocases containing novel adaptations for the sub-organellar location. This review focuses on the evolutionarily conserved chloroplast twin arginine transport (cpTat) pathway. An overview is provided of known aspects of the cpTat components, energy requirements, and mechanisms with a focus on recent discoveries. Some of the most exciting new studies have been in determining the structural architecture of the membrane complex involved in forming the point of passage for the precursor and binding features of the translocase components. The cpTat system is of particular interest because it transports folded protein domains using only the proton motive force for energy. In summary, the implications for mechanism of translocation by recent studies focusing on interactions between membrane Tat components and with the translocating precursor will be discussed.},
doi = {10.1007/s11120-018-0567-z},
journal = {Photosynthesis Research},
number = 3,
volume = 138,
place = {United States},
year = {Sun Aug 12 00:00:00 EDT 2018},
month = {Sun Aug 12 00:00:00 EDT 2018}
}
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