A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase

Journal of Cell Biology

Volumn 157, Issue 2, 2002, Pages 205-210

  Mori, Hiroki ^a   Cline, Kenneth ^a  

^a UNIVERSITY OF FLORIDA   (United States)

Author keywords

Chloroplast; Membrane protein assembly; Sec independent; Tat protein transport; Thylakoid protein transport

Indexed keywords

ARGININE; CARRIER PROTEIN; PROTEIN PRECURSOR; SIGNAL PEPTIDE;

ARTICLE; COMPLEX FORMATION; CROSS LINKING; IMMUNOBLOTTING; IMMUNOPRECIPITATION; NONHUMAN; PEA; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN TRANSPORT; THYLAKOID;

ARGININE; CROSS-LINKING REAGENTS; DIPEPTIDES; ESCHERICHIA COLI PROTEINS; HYDROGEN-ION CONCENTRATION; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MODELS, BIOLOGICAL; PEAS; PLANT PROTEINS; PLASMIDS; PROTEIN BINDING; PROTEIN SORTING SIGNALS; PROTEIN TRANSPORT; THYLAKOIDS; TIME FACTORS;

PISUM SATIVUM;

EID: 0037092039     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200202048     Document Type: Article

References (24)

1. The Tat protein export pathway
2. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
3. A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the ΔpH-dependent thylakoidal protein translocase
4. A folded protein can be transported across the chloroplast envelope and thylakoid membranes
5. Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
6. Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP
7. Multiple pathways for protein transport into or across the thylakoid membrane
8. Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway
9. Targeting determinants and proposed evolutionary basis for the Sec and the Delta pH protein transport systems in chloroplast thylakoid membranes
10. The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane
11. Precursors bind to specific sites on thylakoid membranes prior to transport on the Delta pH protein translocation system
12. Escherichia coli translocase: The untaveling of a molecular machine
13. Chloroplast Oxalp homolog albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes
14. A signal peptide that directs non-Sec transport in bacteria also directs efficient and exclusive transport on the thylakoid Delta pH pathway
15. Post-translational protein translocation into thylakoids by the Sec and Delta pH-dependent pathways
16. Component specificity for the thylakoid Sec and ΔpH-dependent protein transport pathways
17. Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport
18. Dynamics of the TOM complex of mitochondria during binding and translocation of preproteins
19. Structural changes linked to proton translocation by subunit c of the ATP synthase
20. Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure
21. Sec-independent protein translocation by the maize Hcf106 protein
22. Energy-transducing thylakoid membranes remain highly impermeable to ions during protein translocation
23. The maize tha4 gene functions in Sec-independent protein transport in chloroplasts and is related to Hcf106, TatA, and TatB
24. Bacterial twin-arginine signal peptide-dependent protein translocation pathway: Evolution and mechanism