Abstract
Vesicle-inducing protein in plastids 1 (Vipp1) is thought to play an important role both in thylakoid biogenesis and chloroplast envelope maintenance during stress. Vipp1 is conserved in photosynthetic organisms and forms a high homo-oligomer complex structure that may help sustain the membrane integrity of chloroplasts. This study cloned two novel VIPP1 genes from Triticum urartu and named them TuVipp1 and TuVipp2. Both proteins shared high identity with the homologous proteins AtVipp1 and CrVipp1. TuVipp1 and TuVipp2 were expressed in various organs of common wheat, and both genes were induced by light and various stress treatments. Purified TuVipp1 and TuVipp2 proteins showed secondary and advanced structures similar to those of the homologous proteins. Similar to AtVipp1, TuVipp1 is a chloroplast target protein. Additionally, TuVipp1 was able to rescue the phenotypes of pale leaves, lethality, and disordered chloroplast structures of AtVipp1 (-/-) mutant lines. Collectively, our data demonstrate that TuVipp1 and TuVipp2 are functional proteins in chloroplasts in wheat and may be critical for maintaining the chloroplast envelope under stress and membrane biogenesis upon photosynthesis.
Highlights
Thylakoids are vital inner membrane systems of cyanobacteria and chloroplasts in which the major complexes associated with oxygenic photosynthesis are found
Because Vesicle-inducing protein in plastids 1 (Vipp1) functions in thylakoid formation and stress resistance in model plants, we aimed to determine the functions of Vipp1 in crops such as wheat
The primary amino acid sequence of the N terminus of Vipp1 is conserved from E. coli. to higher plants, while that of the C terminus varies
Summary
Thylakoids are vital inner membrane systems of cyanobacteria and chloroplasts in which the major complexes associated with oxygenic photosynthesis are found. Oxygenic photosynthesis complexes are well characterized, but the biogenesis of thylakoids remains obscure. Pigments and proteins are not synthesized in thylakoid membranes; plants develop a series of lipid and protein transport networks in chloroplasts. A protein of 30 kDa was first identified in pea chloroplasts located on both the envelope and thylakoid membranes. This protein was suggested as a candidate for transporting substances (such as pigments, proteins, and lipids) to thylakoids [4].
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