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J Biol Chem, Vol. 275, Issue 3, 1529-1532, January 21, 2000

ACCELERATED PUBLICATION
Chloroplast Oxa1p Homolog Albino3 Is Required for Post-translational Integration of the Light Harvesting Chlorophyll-binding Protein into Thylakoid Membranes^*

Misty Moore, M. Stephen Harrison, Eric C. Peterson, and Ralph Henry

From the Biological Sciences Department, University of Arkansas, Fayetteville, Arkansas 72701

Multiple sorting pathways operate in chloroplasts to localize proteins to the thylakoid membrane. The signal recognition particle (SRP) pathway in chloroplasts employs the function of a signal recognition particle (cpSRP) to target light harvesting chlorophyll-binding protein (LHCP) to the thylakoid membrane. In assays that reconstitute stroma-dependent LHCP integration in vitro, the stroma is replaceable by the addition of GTP, cpSRP, and an SRP receptor homolog, cpFtsY. Still lacking is an understanding of events that take place at the thylakoid membrane including the identification of membrane proteins that may function at the level of cpFtsY binding or LHCP integration. The identification of Oxa1p in mitochondria, an inner membrane translocase component homologous to predicted proteins in bacteria and to the albino3 (ALB3) protein in thylakoids, led us to investigate the potential role of ALB3 in LHCP integration. Antibody raised against a 50-amino acid region of ALB3 (ALB3-50aa) identified a single 45-kDa thylakoid protein. Treatment of thylakoids with antibody to ALB3-50aa inhibited LHCP integration, whereas the same antibody treatment performed in the presence of antigen reversed the inhibition. In contrast, transport by the thylakoid Sec or Delta pH pathways was unaffected. These data support a model whereby a distinct translocase containing ALB3 is used to integrate LHCP into thylakoid membranes.

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^* This work was supported by a fellowship from the Howard Hughes Medical Institute (0412-68022-10-1003 to M. S. H.) 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.

To whom correspondence should be addressed: 601 SCEN, Biological Sciences Dept., University of Arkansas, Fayetteville, AR 72701. Tel.: 501-575-2529; Fax: 501-575-4010; E-mail: rahenry@comp.uark.edu.

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Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

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