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Deletion of FtsH11 protease has impact on chloroplast structure and function in Arabidopsis thaliana when grown under continuous light
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry. Bioinformatics Infrastructure for Life Sciences (BILS), Linköping, Sweden.
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2016 (English)In: Plant, Cell and Environment, ISSN 0140-7791, E-ISSN 1365-3040, Vol. 39, no 11, 2530-2544 p.Article in journal (Refereed) Published
Abstract [en]

The membrane-integrated metallo-protease FtsH11 of Arabidopsis thaliana is proposed to be dual targeted to mitochondria and chloroplasts. A bleached phenotype was observed in ftsh11 grown at long days or continuous light, pointing to disturbances in the chloroplast. Within the chloroplast FtsH11 was found to be located exclusively in the envelope. Two chloroplast-located proteins of unknown function (Tic22-like protein and YGGT-A) showed significantly higher abundance in envelope membranes and intact chloroplasts of ftsH11, and therefore qualify as potential substrates for the FtsH11 protease. No proteomic changes were observed in the mitochondria of 6 weeks old ftsH11 compared to wild type and FtsH11 was not immunodetected in these organelles. The abundance of plastidic proteins, especially of photosynthetic proteins, was altered even during standard growth conditions in total leaves of ftsh11. At continuous light the amount of PSI decreased relative to PSII, accompanied by a drastic change of the chloroplast morphology and a drop of NPQ. FtsH11 is crucial for chloroplast structure and function during growth in prolonged photoperiod.

Place, publisher, year, edition, pages
John Wiley & Sons, 2016. Vol. 39, no 11, 2530-2544 p.
Keyword [en]
envelope, light acclimation
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:umu:diva-124441DOI: 10.1111/pce.12808ISI: 000385842400015PubMedID: 27479913OAI: oai:DiVA.org:umu-124441DiVA: diva2:952021
Available from: 2016-08-11 Created: 2016-08-11 Last updated: 2016-12-09Bibliographically approved
In thesis
1. Characterization of auxiliary membrane proteins in the chloroplast of Arabidopsis thaliana
Open this publication in new window or tab >>Characterization of auxiliary membrane proteins in the chloroplast of Arabidopsis thaliana
2016 (English)Doctoral thesis, comprehensive summary (Other academic)
Alternative title[sv]
Karakterisering av membran-lokaliserade hjälparproteiner i kloroplasten hos växten backtrav
Abstract [en]

In nature, sessile plants have to adapt to their environment and to the never ending changes they are exposed to. They do so mainly by proteomic and metabolomic changes. In all cells, there are complex networks of auxiliary proteins that are responsible for quality control of all the cell's proteins. The auxiliary proteins are divided into chaperones and proteases, and these are further separated into different groups. Chaperones help other proteins in terms of stability and folding. In order for a protein to achieve its function, the three-dimensional structure has to be precise. A protease is a helper protein that is able to break peptide bonds in a process termed proteolysis. Chaperones and proteases can work independently, but sometimes the chaperone unfolds the substrate of the protease to ensure full degradation of the protein. In some cases, the chaperone and the protease functions are combined in one protein.

All proteins studied within this thesis are localized in the chloroplast, the organelle that originated from cyanobacteria, in which plants and algae convert the energy from sunlight into carbohydrates in the process called photosynthesis. Molecular oxygen is released as a by-product, and carbon dioxide is consumed. Photosystem II (PSII), one of the major protein complexes involved in photosynthesis, consists of more than 30 protein subunits, where around half of them are termed low molecular weight (LMW) proteins with a molecular size less than 10 kDa. In this thesis, data identifying one PSII LMW protein, PsbY, as a chaperone for the PSII subcomplex Cytochrome b559 are presented. In the absence of PsbY, Arabidopsis plants were more sensitive to photoinhibition, and the protective circular electron transport around PSII is completely blocked.

Data on members of the Filamentation temperature sensitive protein H (FtsH) protease family are also discussed, with a focus on FtsH11 and FtsHi1-i5. Members of the FtsH protease family carry a protease domain and a chaperone domain. Our data show that FtsH11 has an influence on the structure and function of chloroplasts of Arabidopsis plants grown under continuous light along with protein import into the same. FtsHi1-5 are five members with mutations within the proteolytic motif, most probably rendering them proteolytically inactive, hence they are referred to as ''inactive FtsH proteases''. Knock-out plants of the inactive members are embryo lethal, and knock-down plants grow slower than wild type, probably because of an affected level of plastid proteins at the translational level.

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2016. 52 p.
Keyword
Arabidopsis, chaperone, chloroplast, Cytochrome b559, FtsH, membrane proteins, photosynthesis, Photosystem II, protease, PsbY., Arabidopsis, chaperone, Cytochrome b559, fotosyntes, fotosystem II, FtsH, kloroplast, membranprotein, proteas, PsbY.
National Category
Biochemistry and Molecular Biology Plant Biotechnology
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-125819 (URN)978-91-7601-480-6 (ISBN)
Public defence
2016-10-10, N450, Naturvetarhuset, Umeå, 10:00 (English)
Opponent
Supervisors
Funder
Swedish Energy Agency, 2012-005889​
Note

Avhandlingen är skriven på engelska, men innehåller också en enkel sammanfattning på svenska. 

Available from: 2016-09-26 Created: 2016-09-19 Last updated: 2016-09-23Bibliographically approved

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