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Review
. 2014 Aug:137:100-6.
doi: 10.1016/j.jphotobiol.2014.02.012. Epub 2014 Mar 4.

Quality control of Photosystem II: the molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes

Miho Yoshioka-Nishimura  1 , Yasusi Yamamoto  2
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Free article
Review

Quality control of Photosystem II: the molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes

Miho Yoshioka-Nishimura et al. J Photochem Photobiol B. 2014 Aug.
Free article

Abstract

The reaction center-binding D1 protein of Photosystem II is damaged by excessive light, which leads to photoinhibition of Photosystem II. The damaged D1 protein is removed immediately by specific proteases, and a metalloprotease FtsH located in the thylakoid membranes is involved in the proteolytic process. According to recent studies on the distribution and organization of the protein complexes/supercomplexes in the thylakoid membranes, the grana of higher plant chloroplasts are crowded with Photosystem II complexes and light-harvesting complexes. For the repair of the photodamaged D1 protein, the majority of the active hexameric FtsH proteases should be localized in close proximity to the Photosystem II complexes. The unstacking of the grana may increase the area of the grana margin and facilitate easier access of the FtsH proteases to the damaged D1 protein. These results suggest that the structural changes of the thylakoid membranes by light stress increase the mobility of the membrane proteins and support the quality control of Photosystem II.

Keywords: FtsH protease; Grana; Light stress; Photosystem II; Thylakoid.

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