A protein designated as VIPP1 is found widely in organisms performing oxygenic photosynthesis, but its precise role in chloroplasts has remained somewhat mysterious. Based on its structural similarity, it presumably has evolved from bacterial Phage shock protein A (PspA) with a C-terminal extension of approximately 40 amino acids. Both VIPP1 and PspA are membrane-associated despite the lack of transmembrane helices. They form an extremely large homo-complex that consists of an oligomeric ring unit. Although PspA is known to respond to membrane stress and although it acts in maintaining proton motive force through membrane repair, the multiple function of VIPP1, such as vesicle budding from inner envelope to deliver lipids to thylakoids, maintenance of photosynthetic complexes in thylakoid membranes, biogenesis of Photosystem I, and protective role of inner envelope against osmotic stress, has been proposed. Whatever its precise function in chloroplasts, it is an important protein because depletion of VIPP1 in mutants severely affects photoautotrophic growth. Recent reports of the relevant literature describe that VIPP1 becomes highly mobile when chloroplasts receive hypotonic stress, and that VIPP1 is tightly bound to lipids, which implies a crucial role of VIPP1 in membrane repair through lipid transfer. This review presents a summary of our current knowledge related to VIPP1, particularly addressing the dynamic behavior of complexes against stress and its property of lipid binding. Those data altogether suggest that VIPP1 acts a priori in chloroplast membrane maintenance through its activity to transfer lipids rather than in thylakoid formation through vesicles. This article is part of a Special Issue titled: Chloroplast Biogenesis.
Keywords: Chloroplast; Cyanobacteria; Envelope membrane; Lipid transfer; Thylakoid membrane; Vesicle-inducing protein in plastid 1.
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