distinct pathways mediate the sorting of tail-anchored proteins to the plastid outer envelope不同的途径调解排序tail-anchored蛋白质体外层信封.pdfVIP

Distinct Pathways Mediate the Sorting of Tail-Anchored Proteins to the Plastid Outer Envelope 1 1 2 1 Preetinder K. Dhanoa , Lynn G. L. Richardson , Matthew D. Smith , Satinder K. Gidda , Matthew P. A. 3 3 1 Henderson , David W. Andrews , Robert T. Mullen * 1 Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada, 2 Department of Biology, Wilfrid Laurier University, Waterloo, Ontario, Canada, 3 Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada Abstract Background: Tail-anchored (TA) proteins are a distinct class of membrane proteins that are sorted post-translationally to various organelles and function in a number of important cellular processes, including redox reactions, vesicular trafficking and protein translocation. While the molecular targeting signals and pathways responsible for sorting TA proteins to their correct intracellular destinations in yeasts and mammals have begun to be characterized, relatively little is known about TA protein biogenesis in plant cells, especially for those sorted to the plastid outer envelope. Methodology/Principal Findings: Here we investigated the biogenesis of three plastid TA proteins, including the 33-kDa and 34-kDa GTPases of the translocon at the outer envelope of chloroplasts (Toc33 and Toc34) and a novel 9-kDa protein of unknown function that we define here as an outer envelope TA protein (OEP9). Using a combination of in vivo and in vitro assays we show that OEP9 utilizes a different sorting pathway than that used by Toc33 and Toc34. For instance, while all three TA proteins interact with the cytosolic OEP chaperone/receptor, AKR2A, the plastid targeti