有哪些信誉好的足球投注网站degradation of psbo by the deg protease hhoa is thioredoxin dependent度蛋白酶hhoa psbo退化的硫氧还蛋白相关的.pdfVIP
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degradation of psbo by the deg protease hhoa is thioredoxin dependent度蛋白酶hhoa psbo退化的硫氧还蛋白相关的
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent ¤ Irma N. Roberts , Xuan Tam Lam, Helder Miranda, Thomas Kieselbach, Christiane Funk* ˚ ˚ ˚ Department of Chemistry and Umea Plant Science Centre, Umea University, Umea, Sweden Abstract The widely distributed members of the Deg/HtrA protease family play an important role in the proteolysis of misfolded and damaged proteins. Here we show that the Deg protease rHhoA is able to degrade PsbO, the extrinsic protein of the Photosystem II (PSII) oxygen-evolving complex in Synechocystis sp. PCC 6803 and in spinach. PsbO is known to be stable in its oxidized form, but after reduction by thioredoxin it became a substrate for recombinant HhoA (rHhoA). rHhoA cleaved reduced eukaryotic (specifically, spinach) PsbO at defined sites and created distinct PsbO fragments that were not further degraded. As for the corresponding prokaryotic substrate (reduced PsbO of Synechocystis sp. PCC 6803), no PsbO fragments were observed. Assembly to PSII protected PsbO from degradation. For Synechocystis sp. PCC 6803, our results show that HhoA, HhoB, and HtrA are localized in the periplasma and/or at the thylakoid membrane. In agreement with the idea that PsbO could be a physiological substrate for Deg proteases, part of the cellular fraction of the three Deg proteases of Synechocystis sp. PCC 6803 (HhoA, HhoB, and HtrA) was detected in the PSII-enriched membrane fraction. Citation: Roberts IN, Lam XT, Miranda H, Kieselbach T, Funk C (2012) Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent. PLoS ONE 7(9): e45713. doi:10.1371/journal.pone.0045713 ¨ Editor: Frederik Bornke, Friedrich-Alexander-University Erlangen-Nurenberg, Germany Received May 14, 2012
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