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Journal of Experimental Botany, Vol. 51, No. 90001, pp. 369-374, February 2000
© 2000 Oxford University Press

Transport of proteins into and across the thylakoid membrane

Colin Robinson1, Cheryl Woolhead and Wayne Edwards

Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK

The biogenesis of thylakoid proteins is a complex issue that requires the operation of at least four pathways within the chloroplast. Two of the pathways are used for soluble lumenal proteins, where the proteins bear cleavable targeting signals that are recognized by one of two distinct translocases. These pathways differ in fundamental respects. A subset of lumenal proteins are transported in an unfolded state by a typical Sec system, whereas others are transported by a novel class of translocase that appears to function primarily in the transport of fully-folded proteins. Related protein translocases have now been shown to operate in a wide variety of bacterial species, suggesting a widespread requirement for the translocation of folded proteins across biological membranes. Numerous integral membrane proteins are also targeted into the thylakoid membrane, and these too follow at least two distinct routes. Some proteins use a signal recognition particle-dependent pathway that requires GTP and unidentified apparatus in the thylakoid membrane. Others, however, require none of the known targeting factors and may insert spontaneously into the membrane. In this article, the rationale behind this pathway complexity is discussed in relation to the properties of the substrate proteins and the evolutionary origins of the chloroplast.

Key words: Thylakoid, proteins, chloroplast, Sec system, translocase.


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