TAILIEUCHUNG - Báo cáo khoa học: Functional assembly of thylakoid DpH-dependent/Tat protein transport pathway components in vitro

Assembly of the components of the thylakoidDpH-dependent/Tat protein transport machinery was analyzed in vitro. Upon incubation with intact chloroplasts, precur-sors to all three components, Hcf106, cpTatC and Tha4, were imported into the organelle and assembled into char-acteristic endogenous complexes. In particular, all of the imported cpTatC and approximately two-thirds of the imported Hcf106functionally assembled into 700 kDa complexes capable of binding Tat pathway precursor pro-teins. | Eur. J. Biochem. 270 4930-4941 2003 FEBS 2003 doi Functional assembly of thylakoid ApH-dependent Tat protein transport pathway components in vitro Vivian Fincher Carole Dabney-Smith and Kenneth Cline Horticultural Sciences and Plant Molecular and Cellular Biology University of Florida Gainesville USA Assembly of the components of the thylakoid ApH-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 Hcf106 I unclinaally asmmbled ì mo 700 kDa complexes capable of binding Tat pathway precursor proteins. The amounts assembled into thylakoids by this procedure were moderate. However physiological quantities of mature forms of Tha4 and Hcf106were integrated into isolated thylakoids and a significant percentage of the Hcf106 so Ír i eị i í l al was assembldd into the 000 kDa complex. Interestingly a mutant form of Hcf106 in which an invariant transmembrane glutamate was changed to glutamine integrated into the membrane but did not assemble into the receptor complex. Analysis of energy and known pathway component requirements indicated that Hcf106and Tha4 integrate by an unassisted or spontaneous mechanism. The functionality of in vitro integrated Tha4 was verified by its ability to restore transport to thylakoid membranes from the maize tha4 mutant which lacks the Tha4 protein. Development of this functional in vitro assembly assay will facilitate structure-function studies of the thylakoid Tat pathway translocation machinery. Keywords twin arginine protein transport chloroplast TatB sec-independent. Most thylakoid proteins are encoded in the nucleus and synthesized in the cytosol as precursor proteins reviewed in 1 . Studies of a variety of different .

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