Search results for: Yasusi Yamamoto

Items from 1 to 20 out of 26 results

article

Damage to photosystem II by lipid peroxidation products

Pavel Pospíšil, Yasusi Yamamoto

Biochimica et Biophysica Acta (BBA) - General Subjects > 2017 > 1861 > 2 > 457-466

Photosystem II proteins of higher plant chloroplasts are prone to oxidative stress, and most prominently the reaction center-binding D1 protein is damaged under abiotic stress. The reactive oxygen species produced under these stress conditions have been suggested to be responsible for the protein injury.Recently, it has been shown that the primary and secondary products of non-enzymatic and enzymatic...

article

Born in 1949 in postwar Japan

Yasusi Yamamoto

Photosynthesis Research > 2016 > 127 > 1 > 25-32

In this article, I would like to look back at my life as a researcher of photosynthesis. I was born in 1949, and grew up and was educated in postwar Japan in the 1950s and 1960s. I have studied photosynthesis, in particular Photosystem II, after research experiences in the USA and UK. My study of Photosystem II has continued over 43 years until now. Through the present retrospection, I would like...

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

Miho Yoshioka-Nishimura, Yasusi Yamamoto

Journal of Photochemistry & Photobiology, B: Biology > 2014 > 137 > Complete > 100-106

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...

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Quality control of Photosystem II: Where and how does the degradation of the D1 protein by FtsH proteases start under light stress? – Facts and hypotheses

Miho Yoshioka, Yasusi Yamamoto

Journal of Photochemistry & Photobiology, B: Biology > 2011 > 104 > 1-2 > 229-235

Degradation of the reaction center-binding D1 protein of Photosystem II is central in photoinhibition of Photosystem II. In higher plant chloroplasts, Photosystem II complexes are abundant in the grana. It has been suggested that the Photosystem II complexes containing photodamaged D1 protein migrate for their repair from the grana to the non-appressed stroma thylakoids, where the photodamaged D1...

article

Study on the effects of chloride depletion on photosystem II using different chloride depletion methods

Anjana Jajoo, Sonal Mathur, Pooja Mehta, Miho Yoshoika, more

Journal of Bioenergetics and Biomembranes > 2010 > 42 > 1 > 47-53

Chloride is an indispensable factor for the functioning of oxygen evolving complex (OEC) and has protective and activating effects on photosystem II. In this study we have investigated mainly by EPR, the properties of chloride-sufficient, chloride-deficient and chloride-depleted thylakoid membranes and photosystem II enriched membranes from spinach. The results on the effects of different chloride...

article

Erratum to: Study on the effects of chloride depletion on photosystem II using different chloride depletion methods

Anjana Jajoo, Sonal Mathur, Pooja Mehta, Miho Yashioka, more

Journal of Bioenergetics and Biomembranes > 2010 > 42 > 1 > 97-97

The online version of the original article can be found at http://dx.doi.org/10.1007/s10863-009-9260-4 .

article

Quality control of photosystem II: impact of light and heat stresses

Yasusi Yamamoto, Ryota Aminaka, Miho Yoshioka, Mahbuba Khatoon, more

Photosynthesis Research > 2008 > 98 > 1-3 > 589-608

Photosystem II is vulnerable to various abiotic stresses such as strong visible light and heat. Under both stresses, the damage seems to be triggered by reactive oxygen species, and the most critical damage occurs in the reaction center-binding D1 protein. Recent progress has been made in identifying the protease involved in the degradation of the photo- or heat-damaged D1 protein, the ATP-dependent...

article

Quality control of Photosystem II: Cleavage and aggregation of heat-damaged D1 protein in spinach thylakoids

Keisuke Komayama, Mahbuba Khatoon, Daichi Takenaka, Junko Horie, more

BBA - Bioenergetics > 2007 > 1767 > 6 > 838-846

Moderate heat stress (40 °C, 30 min) on spinach thylakoids induced cleavage of the D1 protein, producing an N-terminal 23-kDa fragment, a C-terminal 9-kDa fragment, and aggregation of the D1 protein. A homologue of Arabidopsis FtsH2 protease, which is responsible for degradation of the damaged D1 protein, was abundant in the stroma thylakoids. Two processes occurred in the thylakoids in response to...

article

Post-illumination-related loss of photochemical efficiency of Photosystem II and degradation of the D1 protein are temperature-dependent

Munna Singh, Yasusi Yamamoto, Kimiyuki Satoh, Eva-Mari Aro, more

Journal of Plant Physiology > 2005 > 162 > 11 > 1246-1253

Photosystem II (PSII) photochemical efficiency (chlorophyll fluorescence ratio Fv/Fm) was recorded in vivo in Synechocystis 6803 during high light illumination and during a subsequent shift of the cells to darkness. A continuing decrease in the Fv/Fm ratio was observed even after the cells were transferred to darkness, provided the temperature was high enough. The decrease in the PSII efficiency after...

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Pressure Equilibrium and Jump Study on Unfolding of 23-kDa Protein from Spinach Photosystem II

Cui-Yan Tan, Chun-He Xu, Jun Wong, Jian-Ren Shen, more

Biophysical Journal > 2005 > 88 > 2 > 1264-1275

Pressure-induced unfolding of 23-kDa protein from spinach photosystem II has been systematically investigated at various experimental conditions. Thermodynamic equilibrium studies indicate that the protein is very sensitive to pressure. At 20°C and pH 5.5, 23-kDa protein shows a reversible two-state unfolding transition under pressure with a midpoint near 160MPa, which is much lower than most natural...

article

Quality control of Photosystem II under light stress – turnover of aggregates of the D1 protein in vivo

Satoshi Ohira, Noriko Morita, Hwa-Jin Suh, Jin Jung, more

Photosynthesis Research > 2005 > 84 > 1-3 > 29-33

When photodamaged under excessive light, the D1 protein is digested and removed from Photosystem (PS) II to facilitate turnover of the protein. In vitro studies have shown that part of the photodamaged D1 protein forms aggregates with surrounding polypeptides before being digested by a protease(s) in the stroma [Yamamoto Y (2001) Plant Cell Physiol 42: 121–128]. The aim of this study was to examine...

article

Chemical Modification of Amine Groups on PS II Protein(s) Retards Photoassembly of the Photosynthetic Water-Oxidizing Complex ^†

Yasuo Ishikawa, Yasusi Yamamoto, Mayuko Otsubo, Steven M. Theg, more

Biochemistry > 2002 > 41 > 6 > 1972 - 1980

article

Characterization of the stromal protease(s) degrading the cross-linked products of the D1 protein generated by photoinhibition of photosystem II

Ali Ferjani, Saori Abe, Yasuo Ishikawa, Takahiro Henmi, more

BBA - Bioenergetics > 2001 > 1503 > 3 > 385-395

When photosystem (PS) II-enriched membranes are exposed to strong light, cross-linking of the intrinsic D1 protein with the surrounding polypeptides and degradation of the D1 protein take place. The cross-linking of the D1 protein with the α-subunit of cytochrome b ₅ ₅ ₉ is suggested to be an early event of photoinduced damage to the D1 protein (Barbato et al., FEBS Lett. 309 (1992)...

article

Protein Translocation within Chloroplast Is Similar in Euglena and Higher Plants

Junko Inagaki, Yuichi Fujita, Toshiharu Hase, Yasusi Yamamoto

Biochemical and Biophysical Research Communications > 2000 > 277 > 2 > 436-442

It is currently thought that chloroplasts of higher plants were derived from endosymbiont oxygenic photosynthetic bacteria (primary endosymbiosis), while Euglena, a photosynthetic protista, gained chloroplasts by secondary endosymbiosis (i.e., incorporation of a photosynthetic eukaryote into heterotrophic eukaryotic host). To examine if the protein transport inside chloroplasts is similar between...

article

Turnover of the aggregates and cross-linked products of the D1 protein generated by acceptor-side photoinhibition of photosystem II

Yasuo Ishikawa, Etsuko Nakatani, Takahiro Henmi, Ali Ferjani, more

BBA - Bioenergetics > 1999 > 1413 > 3 > 147-158

It is known that the reaction-center binding protein D1 in photosystem (PS) II is degraded significantly during photoinhibition. The D1 protein also cross-links covalently or aggregates non-covalently with the nearby polypeptides in PS II complexes by illumination. In the present study, we detected the adducts between the D1 protein and the other reaction-center binding protein D2 (D1/D2), the α-subunit...

article

Secondary structure and thermal stability of the extrinsic 23 kDa protein of photosystem II studied by Fourier transform infrared spectroscopy

Haoming Zhang, Yasuo Ishikawa, Yasusi Yamamoto, Robert Carpentier

FEBS Letters > 1998 > 426 > 3 > 347-351

The secondary structure and thermal stability of the extrinsic 23 kDa protein (OEC23) of spinach photosystem II have been characterized in solution between 25 and 75°C using Fourier transform infrared spectroscopy. Quantitative analysis of the amide I band (1700-1600 cm ^- ¹ ) shows that OEC23 contains 5% α-helix, 37% β-sheet, 24% turn, and 34% disorder structures at 25°C. No appreciable...

article

A Fourier transform infrared spectroscopic study of the effects of hydrogen peroxide and high light on protein conformations of Photosystem II

Haoming Zhang, Yasusi Yamamoto, Yasuo Ishikawa, Weila Zhang, more

Photosynthesis Research > 1997 > 52 > 3 > 215-223

Degradation of the reaction center-binding protein D1 of Photosystem II (PS II) during photoinhibition is dependent on the action of active oxygen species and/or D1-specific proteases. Protein conformational changes may be involved in the process of D1 degradation. In the present study, we determined the effect of H₂O₂ on spinach PS II-enriched membranes and core complexes with respect to electron...

article

Unassembled subunits of the photosynthetic oxygen-evolving complex present in the thylakoid lumen are long-lived and assembly-competent

Akiko Hashimoto, Yasusi Yamamoto, Steven M. Theg

FEBS Letters > 1996 > 391 > 1-2 > 29-34

Physiologically healthy pea chloroplasts contain unassembled, soluble subunits of the oxygen-evolving complex in the thylakoid lumen. We report that the lifetimes of two of these subunits, both on and off the membrane, exceed 8 h in vitro. We also demonstrate that each of the subunits present in the thylakoid lumen is competent for assembly into the membrane-bound complex. These data are consistent...

article

Further characterization of the loss of antenna chlorophyll-binding protein CP43 from Photosystem II during donor-side photoinhibition

Hiroki Mori, Yoriko Yamashita, Tatsuya Akasaka, Yasusi Yamamoto

BBA - Bioenergetics > 1995 > 1228 > 1 > 37-42

The photo-induced reduction in the level of the antenna chlorophyll-binding proteins CP43 and CP47, as well as the reaction-center-forming protein D1, in Photosystem II was studied with PS II membranes and PS II complexes that had been treated with alkaline Tris. The loss of CP43, as detected by sodium dodecyl sulfate/urea polyacrylamide gel electrophoresis, was attributed mostly to specific cross-linking...

article

Isolation of photosystem II reaction center complex by affinity chromatography with the peripheral 33-kDa polypeptide as ligand

Yasuhiro Isogai, Yasusi Yamamoto, Yasuyuki Yamamoto, Mitsuo Nishimura

FEBS Letters > 1987 > 224 > 1 > 71-74

We report a procedure for one-step isolation of the PS II reaction center complex from PS II particles by affinity chromatography with the peripheral 33-kDa polypeptide as ligand. The CaCl ₂ -washed PS II particles prepared from spinach chloroplasts were solubilized with n-octyl-β-d-glucopyranoside and subjected to affinity chromatography. The purified complex consisted of polypeptides with...

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Search results for: Yasusi Yamamoto

Damage to photosystem II by lipid peroxidation products

Born in 1949 in postwar Japan

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

Quality control of Photosystem II: Where and how does the degradation of the D1 protein by FtsH proteases start under light stress? – Facts and hypotheses

Study on the effects of chloride depletion on photosystem II using different chloride depletion methods

Erratum to: Study on the effects of chloride depletion on photosystem II using different chloride depletion methods

Quality control of photosystem II: impact of light and heat stresses

Quality control of Photosystem II: Cleavage and aggregation of heat-damaged D1 protein in spinach thylakoids

Post-illumination-related loss of photochemical efficiency of Photosystem II and degradation of the D1 protein are temperature-dependent

Pressure Equilibrium and Jump Study on Unfolding of 23-kDa Protein from Spinach Photosystem II

Quality control of Photosystem II under light stress – turnover of aggregates of the D1 protein in vivo

Chemical Modification of Amine Groups on PS II Protein(s) Retards Photoassembly of the Photosynthetic Water-Oxidizing Complex ^†

Characterization of the stromal protease(s) degrading the cross-linked products of the D1 protein generated by photoinhibition of photosystem II

Protein Translocation within Chloroplast Is Similar in Euglena and Higher Plants

Turnover of the aggregates and cross-linked products of the D1 protein generated by acceptor-side photoinhibition of photosystem II

Secondary structure and thermal stability of the extrinsic 23 kDa protein of photosystem II studied by Fourier transform infrared spectroscopy

A Fourier transform infrared spectroscopic study of the effects of hydrogen peroxide and high light on protein conformations of Photosystem II

Unassembled subunits of the photosynthetic oxygen-evolving complex present in the thylakoid lumen are long-lived and assembly-competent

Further characterization of the loss of antenna chlorophyll-binding protein CP43 from Photosystem II during donor-side photoinhibition

Isolation of photosystem II reaction center complex by affinity chromatography with the peripheral 33-kDa polypeptide as ligand

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