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Originally published In Press as doi:10.1074/jbc.M106523200 on August 27, 2001

J. Biol. Chem., Vol. 276, Issue 44, 40841-40846, November 2, 2001
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Distinct Albino3-dependent and -independent Pathways for Thylakoid Membrane Protein Insertion*

Cheryl A. WoolheadDagger §, Simon J. ThompsonDagger , Misty Moore, Christophe TissierDagger , Alexandra MantDagger ||, Alison Rodger§, Ralph Henry, and Colin RobinsonDagger **

From the Dagger  Department of Biological Sciences and § Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom and  Biological Science Department, University of Arkansas, Fayetteville, Arkansas 72701

The homologous proteins Oxa1, YidC, and Alb3 mediate the insertion of membrane proteins in mitochondria, bacteria, and chloroplast thylakoids, respectively. Depletion of YidC in Escherichia coli affects the integration of every membrane protein studied, and Alb3 has been shown previously to be required for the insertion of a signal recognition particle (SRP)-dependent protein, Lhcb1, in thylakoids. In this study we have analyzed the "global" role of Alb3 in the insertion of thylakoid membrane proteins. We show that insertion of two chlorophyll-binding proteins, Lhcb4.1 and Lhcb5, is almost totally blocked by preincubation of thylakoids with anti-Alb3 antibodies, indicating a requirement for Alb3 in the insertion pathway. Insertion of the related PsbS protein, on the other hand, is unaffected by Alb3 antibodies, and insertion of a group of SRP-independent, signal peptide-bearing proteins, PsbX, PsbW, and PsbY, is likewise completely unaffected. Proteinase K is furthermore able to completely degrade Alb3, but this treatment does not affect the insertion of these proteins. Among the thylakoid proteins studied here, Alb3 requirement correlates strictly with a requirement for stromal factors and nucleoside triphosphates. However, the majority of proteins tested do not require Alb3 or any other known form of translocation apparatus.

* This work was supported by an Engineering and Physical Sciences Research Council studentship (to C. A. W.), by an EPSRC Biosciences Interface Network Grant GR/M91105 (to A. R. and C. R.), by Biotechnology and Biological Sciences Research Council Grants C07900 and C12908 (to C. R.), and by National Science Foundation Grant MCB-9807826 (to R. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| Present address: Plant Biochemistry Laboratory, Dept. of Plant Biology, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark.

** To whom correspondence should be addressed. Tel.: 44 2476 523557; Fax: 44 2476 523568; E-mail: Crobinson@bio.warwick.ac.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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