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ID 55382
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Yoshioka-Nishimura, Miho Graduate School of Natural Science and Technology, Okayama University
Nanba, Daisuke Graduate School of Natural Science and Technology, Okayama University
Takaki, Takashi Techinical support center, JEOL
Ohba, Chikako Graduate School of Natural Science and Technology, Okayama University
Tsumura, Nodoka Graduate School of Natural Science and Technology, Okayama University
Morita, Noriko Graduate School of Natural Science and Technology, Okayama University
Sakamoto, Hirotaka Ushimado Marine Institute, Okayama University ORCID Kakenhi publons
Murata, Kazuyoshi National Institute for Physiological Sciences
Yamamoto, Yasusi Graduate School of Natural Science and Technology, Okayama University
Abstract
 Under light stress, the reaction center-binding protein D1 of PSII is photo-oxidatively damaged and removed from PSII complexes by proteases located in the chloroplast. A protease considered to be responsible for degradation of the damaged D1 protein is the metalloprotease FtsH. We showed previously that the active hexameric FtsH protease is abundant at the grana margin and the grana end membranes, and this homo-complex removes the photodamaged D1 protein in the grana. Here, we showed a change in the distribution of FtsH in spinach thylakoids during excessive illumination by transmission electron microscopy (TEM) and immunogold labeling of FtsH. The change in distribution of the protease was accompanied by structural changes to the thylakoids, which we detected using spinach leaves by TEM after chemical fixation of the samples. Quantitative analyses showed several characteristic changes in the structure of the thylakoids, including shrinkage of the grana, outward bending of the marginal portions of the thylakoids and an increase in the height of the grana stacks under excessive illumination. The increase in the height of the grana stacks may include swelling of the thylakoids and an increase in the partition gaps between the thylakoids. These data strongly suggest that excessive illumination induces partial unstacking of the thylakoids, which enables FtsH to access easily the photodamaged D1 protein. Finally three-dimensional tomography of the grana was recorded to observe the effect of light stress on the overall structure of the thylakoids.
Keywords
FtsH protease
Light stress
Photosystem II
Spinach chloroplast
TEM
Thylakoid
Note
This is an Accepted Manuscript of an article published by Oxford University Press
Published Date
2014-07-01
Publication Title
Plant and Cell Physiology
Volume
volume55
Issue
issue7
Publisher
Japanese Society of Plant Physiologists
Start Page
1255
End Page
1265
ISSN
0032-0781
NCID
AA0077511X
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
Copyright Holders
https://creativecommons.org/licenses/by-nc-nd/4.0/deed.ja
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Related Url
https://doi.org/10.1093/pcp/pcu079