Thylakoid targeting of Tat passenger proteins shows no DeltapH dependence in vivo

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Functional assembly of thylakoid deltapH-dependent/Tat protein transport pathway components in vitro.

Assembly of the components of the thylakoid deltapH-dependent/Tat protein transport machinery was analyzed in vitro. Upon incubation with intact chloroplasts, precursors to all three components, Hcf106, cpTatC and Tha4, were imported into the organelle and assembled into characteristic endogenous complexes. In particular, all of the imported cpTatC and approximately two-thirds of the imported H...

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Proton transfer limits protein translocation rate by the thylakoid DeltapH/Tat machinery.

The thylakoid transmembrane DeltapH is the sole energy source driving translocation of precursor proteins by the DeltapH/Tat machinery. Consequently, proton translocation must be coupled to precursor translocation. For the precursor of the 17 kDa protein of the oxygen-evolving complex (pOE17), the protein translocation process is characterized by a steep drop in efficiency at an external pH bel...

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In vivo transport of folded EGFP by the DeltapH/TAT-dependent pathway in chloroplasts of Arabidopsis thaliana.

Among the protein translocation pathways of the thylakoid membrane in chloroplasts, the DeltapH/TAT pathway is unique in several aspects. In vitro transport assays with isolated chloroplasts or thylakoids have defined the trans-thylakoidal proton gradient as the sole requirement for effecting transport. From these studies, evidence has also accumulated indicating that, in contrast to the remain...

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Large-scale translocation reversal within the thylakoid Tat system in vivo

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ژورنال

عنوان ژورنال: The EMBO Journal

سال: 2003

ISSN: 1460-2075

DOI: 10.1093/emboj/cdg081