NDLI: Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions

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Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions

Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II

Conformational changes and their role in non-radiative energy dissipation in photosystem II reaction centres

Structure and evolution of the extrinsic proteins that stabilize the oxygen-evolving engine

Solving the structure of plant photosystem I—biochemistry is vital

Excitation energy transfer from phycobiliprotein to chlorophyll d in intact cells of Acaryochloris marina studied by time- and wavelength-resolved fluorescence spectroscopy

The assembly and organisation of photosynthetic membranes in Rhodobacter sphaeroides

Isolation and characterization of a xanthophyll-rich fraction from the thylakoid membrane of Dunaliella salina(green algae)

The mechanism for dioxygen formation in PSII studied by quantum chemical methods

A role of the C-terminal extension of the photosystem II D1 protein in sensitivity of the cyanobacterium Synechocystis PCC 6803 to photoinhibition

The role of D1-Ala344 in charge stabilization and recombination in Photosystem II

Kinetic characterisation of the light-driven protochlorophyllide oxidoreductase (POR) from Thermosynechococcus elongatus

The nature of the photosystem II reaction centre in the chlorophyll d-containing prokaryote, Acaryochloris marina

Degradation of the main Photosystem II light-harvesting complex

Functional flexibility and acclimation of the thylakoid membrane

Granal stacking of thylakoid membranes in higher plant chloroplasts: the physicochemical forces at work and the functional consequences that ensue

Photosystem I: a search for green plant trimers

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Photochemical & Photobiological Sciences Vol - 4 Issue - 9

Photochemical & Photobiological Sciences Vol - 4 Issue - 8

Photochemical & Photobiological Sciences Vol - 4 Issue - 7

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Photochemical & Photobiological Sciences Vol - 4 Issue - 5

Photochemical & Photobiological Sciences Vol - 4 Issue - 4

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Photochemical & Photobiological Sciences Vol - 4 Issue - 2

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Photochemical & Photobiological Sciences Vol -2

Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions

Content Provider	Royal Society of Chemistry (RSC)
Author	Shen, Jian-Ren Yamamoto, Yasusi Mann, Nicholas H. Hiramoto, Hideki Morita, Noriko Kamata, Takashi
Copyright Year	2005
Abstract	The role of an AAA protease FtsH (slr0228) in the turnover of the D1 protein was studied under moderate heat stress conditions using wild-type cells of the cyanobacterium Synechocystis PCC 6803 and the mutant cells lacking a homologue of FtsH (slr0228). When the growth temperature of the wild-type was shifted from 30 °C to 40 °C, growth and oxygen-evolving activity were partially inhibited. Under the same heat stress, growth of the mutant was inhibited more significantly (63% inhibition after 5 days heat stress, compared with 26% inhibition with the wild-type cells) and the oxygen-evolving activity was also impaired in parallel. With heat stress at 42 °C, the level of the D1 protein of wild type cells was decreased, whereas that in mutant cells was not. The responses of cyanobacterial cells to heat stress observed here are quite similar to those to light stress that were reported previously [P. Silva, E. Thompson, S. Bailey, O. Kruse, C. W. Mullineaux, C. Robinson, N. H. Mann and P. J. Nixon, Plant Cell, 2003, 15, 2152–2164, ]. From these results, we suggest that the FtsH protease (slr0228) is responsible for both the heat-induced and light-induced degradation of the D1 protein. Notably, the amount of FtsH increased when the wild-type cells were exposed to heat stress or light stress, indicating that the up-regulation of the FtsH protease in the thylakoids is crucial for the cyanobacterial cells to cope with these abiotic stresses.
Starting Page	983
Ending Page	990
Page Count	8
File Format	HTM / HTML PDF
ISSN	1474905X
Volume Number	4
Issue Number	12
Journal	Photochemical & Photobiological Sciences
DOI	10.1039/b506068k
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Nixon Robinson Silva Mullineaux Richard Nixon Synechocystis Protein Mann Protease Michael E. Mann Kruse Cyanobacteria Thompson Bailey
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry

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In vivo quality control of photosystem II in cyanobacteria Synechocystis sp. PCC 6803: D1 protein degradation and repair under the influence of light, heat and darkness

Cellular & molecular biology letters 77 the synechocystis ftsh protease slr0228 is involved in the control of selective d1 turnover as well as cellular level of unassembled cp47 and d2.

psbA gene family coding D1 proteins of photosystem II of cyanobacteria Synechocystis PCC 6803 is essential for DNA repair/protection

The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein.

Computational protein structure modeling and analysis of UV-B stress protein in Synechocystis PCC 6803.

A role of the C-terminal extension of the photosystem II D1 protein in sensitivity of the cyanobacterium Synechocystis PCC 6803 to photoinhibition

Function and association of CyanoP in photosystem II of Synechocystis sp. PCC 6803

Regulation of RNase E during the UV stress response in the cyanobacterium <i>Synechocystis</i> sp. PCC 6803.

The Thylakoid FtsH Protease Plays a Role in the Light-Induced Turnover of the Photosystem II D1 Protein

Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions

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In vivo quality control of photosystem II in cyanobacteria Synechocystis sp. PCC 6803: D1 protein degradation and repair under the influence of light, heat and darkness

Cellular & molecular biology letters 77 the synechocystis ftsh protease slr0228 is involved in the control of selective d1 turnover as well as cellular level of unassembled cp47 and d2.

psbA gene family coding D1 proteins of photosystem II of cyanobacteria Synechocystis PCC 6803 is essential for DNA repair/protection

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Computational protein structure modeling and analysis of UV-B stress protein in Synechocystis PCC 6803.

A role of the C-terminal extension of the photosystem II D1 protein in sensitivity of the cyanobacterium Synechocystis PCC 6803 to photoinhibition

Function and association of CyanoP in photosystem II of Synechocystis sp. PCC 6803

Regulation of RNase E during the UV stress response in the cyanobacterium <i>Synechocystis</i> sp. PCC 6803.

The Thylakoid FtsH Protease Plays a Role in the Light-Induced Turnover of the Photosystem II D1 Protein

Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions