Thylakoid Assembly and Folded Protein Transport by the Tat Pathway
Assembly of functional photosystems complete with necessary intrinsic and extrinsic proteins requires the function of at least three protein transport pathways in thylakoid membranes. Our research focuses on one of those pathways, a unique and essential protein transport pathway found in the chloroplasts of plants, bacteria, and some archaebacteria, the Twin arginine translocation (Tat) system. The chloroplast Tat (cpTat) system is thought to be responsible for the proper localization of ~50% of thylakoid lumen proteins, several of which are necessary for proper photosystem assembly, maintenance, and function. For example, two components of the extrinsic oxygen evolving complex, PsbP and PsbQ, are transported to the thylakoid lumen via the cpTat system. PsbP and PsbQ have been shown to be important in photosystem II function and maintenance (Yi et al. 2006; Yi et al. 2007). The current project addresses the issues of what forms the translocation conduit, how the translocon complex is arranged and what role Hcf106 and cpTatC may have in the process of forming the conduit.
- Research Organization:
- Miami Univ., Oxford, OH (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division
- DOE Contract Number:
- SC0014441
- OSTI ID:
- 1830759
- Report Number(s):
- DOE-MIAMI-0014441
- Country of Publication:
- United States
- Language:
- English
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