| Literature DB >> 25897076 |
Stefanie Tietz1, Sujith Puthiyaveetil1, Heather M Enlow1, Robert Yarbrough1, Magnus Wood1, Dmitry A Semchonok2, Troy Lowry3, Zhirong Li4, Peter Jahns5, Egbert J Boekema2, Steven Lenhert3, Krishna K Niyogi4, Helmut Kirchhoff6.
Abstract
The structural organization of proteins in biological membranes can affect their function. Photosynthetic thylakoid membranes in chloroplasts have the remarkable ability to change their supramolecular organization between disordered and semicrystalline states. Although the change to the semicrystalline state is known to be triggered by abiotic factors, the functional significance of this protein organization has not yet been understood. Taking advantage of an Arabidopsis thaliana fatty acid desaturase mutant (fad5) that constitutively forms semicrystalline arrays, we systematically test the functional implications of protein crystals in photosynthetic membranes. Here, we show that the change into an ordered state facilitates molecular diffusion of photosynthetic components in crowded thylakoid membranes. The increased mobility of small lipophilic molecules like plastoquinone and xanthophylls has implications for diffusion-dependent electron transport and photoprotective energy-dependent quenching. The mobility of the large photosystem II supercomplexes, however, is impaired, leading to retarded repair of damaged proteins. Our results demonstrate that supramolecular changes into more ordered states have differing impacts on photosynthesis that favor either diffusion-dependent electron transport and photoprotection or protein repair processes, thus fine-tuning the photosynthetic energy conversion.Entities:
Keywords: macromolecular crowding; membrane structure; nonphotochemical quenching; photosynthesis; photosystem II; protein crystallization; semicrystalline arrays; thylakoid membrane
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Year: 2015 PMID: 25897076 PMCID: PMC4447980 DOI: 10.1074/jbc.M114.619841
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157