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J Biol Chem, Vol. 274, Issue 17, 12177-12182, April 23, 1999

Chloroplast SecY Is Complexed to SecE and Involved in the Translocation of the 33-kDa but Not the 23-kDa Subunit of the Oxygen-evolving Complex

Danja Schuenemann, Pinky Amin, Enno Hartmann, and Neil E. Hoffman

From the Department of Plant Biology, Carnegie Institution of Washington, Stanford, California 94305 and the  Zentrum Biochemie und Molekulare Zellbiologie, Gosslerstrasse 12d, D-37073 Goettingen, Germany

SecY is a component of the protein-conducting channel for protein transport across the cytoplasmic membrane of prokaryotes. It is intimately associated with a second integral membrane protein, SecE, and together with SecA forms the minimal core of the preprotein translocase. A chloroplast homologue of SecY (cpSecY) has previously been identified and determined to be localized to the thylakoid membrane. In the present work, we demonstrate that a SecE homologue is localized to the thylakoid membrane, where it forms a complex with cpSecY. Digitonin solubilization of thylakoid membranes releases the SecY/E complex in a 180-kDa form, indicating that other components are present and/or the complex is a higher order oligomer of the cpSecY/E dimer. To test whether cpSecY forms the protein-conducting channel of the thylakoid membrane, translocation assays were conducted with the SecA-dependent substrate OE33 and the SecA-independent substrate OE23, in the presence and absence of antibodies raised against cpSecY. The antibodies inhibited translocation of OE33 but not OE23, indicating that cpSecY comprises the protein-conducting channel used in the SecA-dependent pathway, whereas a distinct protein conducting channel is used to translocate OE23.

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