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Published 15 April 2002. doi:10.1083/jcb.200202048
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© The Rockefeller University Press, 0021-9525/2002/4/205 $5.00
The Journal of Cell Biology, Volume 157, Number 2, April 15, 2002 205-210

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

Hiroki Mori and Kenneth Cline

Horticultural Sciences and Plant Molecular and Cellular Biology, University of Florida, Gainesville, FL 32611

Address correspondence to Kenneth Cline, Horticultural Sciences Department, Fifield Hall, University of Florida, Gainesville, FL 32611. Tel.: (352) 392-4711 ext. 219. Fax: (352) 392-5653. E-mail: kcline{at}ufl.edu

The thylakoid {Delta}pH-dependent/Tat pathway is a novel system with the remarkable ability to transport tightly folded precursor proteins using a transmembrane {Delta}pH as the sole energy source. Three known components of the transport machinery exist in two distinct subcomplexes. A cpTatC–Hcf106 complex serves as precursor receptor and a Tha4 complex is required after precursor recognition. Here we report that Tha4 assembles with cpTatC–Hcf106 during the translocation step. Interactions among components were examined by chemical cross-linking of intact thylakoids followed by immunoprecipitation and immunoblotting. cpTatC and Hcf106 were consistently associated under all conditions tested. In contrast, Tha4 was only associated with cpTatC and Hcf106 in the presence of a functional precursor and the {Delta}pH. Interestingly, a synthetic signal peptide could replace intact precursor in triggering assembly. The association of all three components was transient and dissipated upon the completion of protein translocation. Such an assembly–disassembly cycle could explain how the {Delta}pH/Tat system can assemble translocases to accommodate folded proteins of varied size. It also explains in part how the system can exist in the membrane without compromising its ion and proton permeability barrier.

Key Words: thylakoid protein transport; chloroplast; Tat protein transport; Sec independent; membrane protein assembly


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