Biomedical subjects

Kazuhiko Satoh

Publications and source records attributed to Kazuhiko Satoh.

13 recordsLinked to original sources

PubMed2007

Chloroplast-encoded polypeptide PsbT is involved in the repair of primary electron acceptor QA of photosystem II during photoinhibition in Chlamydomonas reinhardtii.

PsbT is a small chloroplast-encoded hydrophobic polypeptide associated with the D1/D2 heterodimer of the photosystem II (PSII) reaction center and is required for the efficient post-translational repair of photodamaged PSII. Here we addressed that role in detail in Chlamydomonas reinhardtii wild type and DeltapsbT cells by analyzing the activities of PSII, the assembly of PSII proteins, and the redox components of PSII during photoinhibition and repair. Strong illumination of cells for 15 min decreased the activities of electron transfer through PSII and Q(A) photoreduction by 50%, and it reduced the amount of atomic manganese by 20%, but it did not affect the steady-state level of PSII proteins, photoreduction of pheophytin (pheo(D1)), and the amount of bound plastoquinone (Q(A)), indicating that the decrease in PSII activity resulted mainly from inhibition of the electron transfer from pheo(D1) to Q(A). In wild type cells, we observed parallel recovery of electron transfer activity through PSII and Q(A) photoreduction, suggesting that the recovery of Q(A) activity is one of the rate-limiting steps of PSII repair. In DeltapsbT cells, the repairs of electron transfer activity through PSII and of Q(A) photoreduction activity were both impaired, but PSII protein turnover was unaffected. Moreover, about half the Q(A) was lost from the PSII core complex during purification. Since PsbT is intimately associated with the Q(A)-binding region on D2, we propose that this polypeptide enhances the efficient recovery of Q(A) photoreduction by stabilizing the structure of the Q(A)-binding region.

Animals↗

PubMed2006

Preparation of membrane proteins for analysis by two-dimensional gel electrophoresis.

In order to separate hydrophobic membrane proteins, we have developed a novel two-dimensional electrophoresis system. For the iso-electric focusing, agarose was used as a supporting matrix and n-dodecyl-beta-D-maltopyranoside was used as a surfactant. In combination with a previously developed Tris/MES electrophoresis system in the second dimension, distinct spots were reproducibly detected from hydrophobic membrane proteins whose grand average hydropathicity (GRAVY) exceed 0.3. In contrast to the immobilized pH gradient system, c-type heme was also visualized in this system.

Bacterial Proteins↗

PubMed2006

Acclimation to the growth temperature and thermosensitivity of photosystem II in a mesophilic cyanobacterium, Synechocystis sp. PCC6803.

Differences in the temperature dependence and thermosensitivities of PSII activities in Synechocystis sp. PCC6803 grown at 25 and 35 degrees C were studied. Hill reactions in cells, thylakoid membranes and purified PSII core complexes were measured at high temperatures or at their growth temperatures after high-temperature treatments. In the presence of 2,5-dichloro-p-benzoquinone as an electron acceptor, which can accept electrons directly from Q(A), the temperature dependence of the oxygen-evolving activity was almost the same in thylakoid membranes and in the purified PSII complexes from cells grown at 25 or 35 degrees C. When duroquinone, which accepts electrons only through Q(B) plastoquinone, was used as an electron acceptor, the temperature dependence was the same for purified PSII core complexes but was different between thylakoids isolated from the cells grown at 25 and 35 degrees C. No remarkable difference was observed in protein compositions between thylakoids and between purified PSII complexes from cells grown at 25 or 35 degrees C. However, the fluidity of thylakoids, measured by electron flow to P700, was affected by the growth temperature. These results suggest that one of the major factors which cause the changes in the thermosensitivity of PSII is the change in the fluidity of thylakoid membranes. As for the acclimation of PSII in thylakoids to high temperatures, one of the main causes is the decrease in the high-temperature-induced formation of non-Q(B) PSII due to the decreased fluidity in the cells grown at 35 degrees C.

Acclimatization↗

PubMed2006

Jaw muscle functional anatomy in northern grasshopper mouse, Onychomys leucogaster, a carnivorous murid.

The jaw muscle anatomy of the northern grasshopper mouse, Onychomys leucogaster, was observed and the mechanical basis of the insectivorous/carnivorous adaptations were examined. Compared with Peromyscus maniculatus, a granivorous relative of Onychomys, there is a reduction of some aponeuroses within the masseter deep layer. This characteristic indicates that shearing meat or crushing arthropod exoskeletons requires less occlusal pressure than does grinding plant material. In Onychomys both the anterior and posterior portions of the masseter deep layer are more anterodorsally inclined, so that the line of action of the masseter lies further from the jaw joint than in Peromyscus. A strong incisal bite for killing vertebrates such as other rodents can be produced by a jaw mechanism with the high lever advantage of this muscle, which compensates for the decline in muscle mass. Our quantitative analysis suggests that the disappearance of an aponeurosis along the zygomatic plate in Onychomys decreases the stretch of the corresponding muscle, i.e., the anterior fibers of the masseter deep layer, accompanying jaw opening, and increases the maximum gape necessary for hunting large prey.

Animals↗

PubMed2005

PsbU provides a stable architecture for the oxygen-evolving system in cyanobacterial photosystem II.

PsbU is a lumenal peripheral protein in the photosystem II (PS II) complex of cyanobacteria and red algae. It is thought that PsbU is replaced functionally by PsbP or PsbQ in plant chloroplasts. After the discovery of PsbP and PsbQ homologues in cyanobacterial PS II [Thornton et al. (2004) Plant Cell 16, 2164-2175], we investigated the function of PsbU using a psbU deletion mutant (DeltaPsbU) of Synechocystis 6803. In contrast to the wild type, DeltaPsbU did not grow when both Ca2+ and Cl- were eliminated from the growth medium. When only Ca2+ was eliminated, DeltaPsbU grew well, whereas when Cl- was eliminated, the growth rate was highly suppressed. Although DeltaPsbU grew normally in the presence of both ions under moderate light, PS II-related disorders were observed as follows. (1) The mutant cells were highly susceptible to photoinhibition. (2) Both the efficiency of light utilization under low irradiance and the chlorophyll-specific maximum rate of oxygen evolution in DeltaPsbU cells were 60% lower than those of the wild type. (3) The decay of the S2 state in DeltaPsbU cells was decelerated. (4) In isolated PS II complexes from DeltaPsbU cells, the amounts of the other three lumenal extrinsic proteins and the electron donation rate were drastically decreased, indicating that the water oxidation system became significantly labile without PsbU. Furthermore, oxygen-evolving activity in DeltaPsbU thylakoid membranes was highly suppressed in the absence of Cl-, and 60% of the activity was restored by NO3- but not by SO4(2-), indicating that PsbU had functions other than stabilizing Cl-. On the basis of these results, we conclude that PsbU is crucial for the stable architecture of the water-splitting system to optimize the efficiency of the oxygen evolution process.

Bacterial Proteins↗

PubMed2004

Internal architecture, origin-insertion site, and mass of jaw muscles in Old World hamsters.

The jaw muscle (i.e., masticatory, suprahyoid, and extrinsic tongue) anatomy and mass were examined in four genera of Old World hamsters (cricetine murids), Mesocricetus, Cricetulus, Tscherskia, and Phodopus. The masseter was the largest and most complicated of the muscles examined. In the superficial layer, a few ventral fibers form a small medially turned portion with an insertion site more similar to those of sciurids than of other murids. In Mesocricetus, the superficial layer has a discrete anteroventral portion that has not been reported for other murid rodents. Examination of the fiber attachment sites indicated that the deep layer contains four parts and the medial layer contains three parts. The deep layer originates from two aponeuroses that are firmly connected to each other at their anterior ends and lie along the zygomatic arch. The aponeurosis of insertion for the deep layer is situated along the masseteric ridge and the dorsal border of the angular process, but is absent in its middle part, consistent with reports in two relatives, sigmodontine and arvicoline murids. In cricetine murids, unlike in other rodents, fibers insert on the dorsal narrow strip of the posterior mandibular aponeurosis, not on its broad medial aspect. The relative mass of some masticatory and suprahyoid muscles is related to body mass. Small species (Cricetulus and Phodopus) have relatively larger masseter and mylohyoid muscles and smaller temporalis and geniohyoid muscles than large species (Mesocricetus and Tscherskia).

Animals↗

PubMed2004

Deactivation of photosynthetic activities is triggered by loss of a small amount of water in a desiccation-tolerant cyanobacterium, Nostoc commune.

Changes in photosynthetic activities under hypertonic conditions were studied in a terrestrial, highly desiccation-tolerant cyanobacterium, Nostoc commune, and in some desiccation-sensitive cyanobacteria. The amounts of water sustained in the colony matrix outside the N. commune cells and the cellular solute concentration were estimated by measuring the water potential, and the solute concentration was supposed to correspond to around 0.22 M sorbitol. Incubation of the colonies in 0.8 M sorbitol solution inhibited the energy transfer from the phycobilisome (PBS) anchor to PSII core complexes. At higher sorbitol concentrations, light energy absorbed by PSI, PSII, and PBS was dissipated to heat. PSI and cyclic electron flow around PSI was also deactivated by hypertonic treatment. Fv/Fm and (Fm'-F)/Fm' values started to decrease at 0.6 and 0.3 M sorbitol and reached zero at 1.0 and 0.8 M, respectively. Decreases in these two fluorescence parameters corresponded to the decreases in PSII fluorescence (F695) and photosynthetic CO2 fixation, respectively. The intensity of delayed light emission started to decrease at 1.0 M sorbitol and became negligible at 4.0 M. Comparing these changes in N. commune with those in desiccation-sensitive species, we found that N. commune cells actively deactivates photosynthetic systems on sensing water loss.

Carbon Dioxide↗

PubMed2004

Inactivation of ycf33 results in an altered cyclic electron transport pathway around photosystem I in Synechocystis sp. PCC6803.

ycf33 encodes a small protein with a molecular mass of 7.5 kDa and is found from cyanobacteria to higher plants. A ycf33 deletion mutant was constructed in Synechocystis sp. PCC6803 and characterized. The mutant showed a higher phycobilisome/chlorophyll ratio than the wild type and a higher photosystem II/photosystem I fluorescence ratio measured at 77 K. Under photoautotrophic conditions, the growth rates were not much different from those of the wild type. Cyclic electron transport activities around photosystem I were not much different between the wild type and the mutant. However, the effects of diphenyleneiodonium, an inhibitor of flavoprotein, on cyclic electron transport in the mutant were different from those in the wild type; it was severely inhibited in the wild type but not much in the mutant. Together with the effects of nitrite, which accepts electrons from ferredoxin via nitrite reductase and those of HgCl2, it was suggested that the pathway of cyclic electron transport is altered in the mutant.

Amino Acid Sequence↗

PubMed2003

Arrest of chlorophyll synthesis and differential decrease of Photosystems I and II in a cyanobacterial mutant lacking light-independent protochlorophyllide reductase.

The chlL gene encodes one subunit of the light-independent protochlorophyllide reductase. A chlL-lacking mutant of the cyanobacterium Plectonema boryanum is unable to synthesize chlorophyll (Chl) in the dark, causing Chl synthesis to become light-dependent as in angiosperms. When the mutant cells were cultivated heterotrophically in the dark, Chl synthesis was arrested and the Chl content decreased exponentially in reverse profile to cell propagation, indicating that most of the pre-existing Chl was recruited for daughter cells. During this 'etiolating' process the Chl content became less than 0.5% of the original level. In parallel to this there was a decrease in the activity of Photosystem I (PSI), the amount of its core Chl-binding subunits, PsaA/PsaB, and a peripheral subunit, PsaC. Levels of transcripts for these subunits were not significantly changed upon the arrest of Chl synthesis. In contrast, Photosystem II (PSII) was maintained to a significant extent in terms of activity and protein levels of D1 and CP47 until a late stage of the etiolation, implying that PSII is newly synthesized though Chl synthesis was arrested. Low-temperature (77 K) fluorescence spectral analysis supported a selective decrease in Chl associated with PSI. Taken together, it is suggested that the pre-existing Chl molecules in periphery of PSI could be released and re-distributed for PSII biosynthesis in the etiolating cyanobacterial cells.

Bacterial Proteins↗

PubMed2002

Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides.

A highly active oxygen-evolving photosystem II (PSII) complex was purified from the HT-3 strain of the widely used cyanobacterium Synechocystis sp. PCC 6803, in which the CP47 polypeptide has been genetically engineered to contain a polyhistidine tag at its carboxyl terminus [Bricker, T. M., Morvant, J., Masri, N., Sutton, H. M., and Frankel, L. K. (1998) Biochim. Biophys. Acta 1409, 50-57]. These purified PSII centers had four manganese atoms, one calcium atom, and two cytochrome b(559) hemes each. Optical absorption and fluorescence emission spectroscopy as well as western immunoblot analysis demonstrated that the purified PSII preparation was devoid of any contamination with photosystem I and phycobiliproteins. A comprehensive proteomic analysis using a system designed to enhance resolution of low-molecular-weight polypeptides, followed by MALDI mass spectrometry and N-terminal amino acid sequencing, identified 31 distinct polypeptides in this PSII preparation. We propose a new nomenclature for the polypeptide components of PSII identified after PsbZ, which proceeds sequentially from Psb27. During this study, the polypeptides PsbJ, PsbM, PsbX, PsbY, PsbZ, Psb27, and Psb28 proteins were detected for the first time in a purified PSII complex from Synechocystis 6803. Five novel polypeptides were also identified in this preparation. They included the Sll1638 protein, which shares significant sequence similarity to PsbQ, a peripheral protein of PSII that was previously thought to be present only in chloroplasts. This work describes newly identified proteins in a highly purified cyanobacterial PSII preparation that is being widely used to investigate the structure, function, and biogenesis of this photosystem.

Arabidopsis Proteins↗

PubMed2002

Recovery of photosynthetic systems during rewetting is quite rapid in a terrestrial cyanobacterium, Nostoc commune.

Recovery processes of photosynthetic systems during rewetting were studied in detail in a terrestrial, highly drought-tolerant cyanobacterium, Nostoc commune. With absorption of water, the weight of N. commune colony increased in three phases with half-increase times of about 1 min, 2 h and 9 h. Fluorescence intensities of phycobiliproteins and photosystem (PS) I complexes were recovered almost completely within 1 min, suggesting that their functional forms were restored very quickly. Energy transfer from allophycocyanin to the core-membrane linker peptide (L(CM)) was recovered within 1 min, but not that from L(CM) to PSII. PSI activity and cyclic electron flow around PSI recovered within 2 min, while the PSII activity recovered in two phases after a time lag of about 5 min, with half times of about 20 min and 2 h. Photosynthetic CO(2) fixation was restored almost in parallel with the first recovery phase of the PSII reaction center activity. Although the amount of absorbed water became more than 20 times the initial dry weight of the N. commune colony in the presence of sufficient water, about twice the initial dry weight was enough for recovery and maintenance of the PSII activity.

Acclimatization↗

PubMed2002

Low-molecular-mass polypeptide components of a photosystem II preparation from the thermophilic cyanobacterium Thermosynechococcus vulcanus.

Using a recently introduced electrophoresis system [Kashino et al. (2001) Electrophoresis 22: 1004], components of low-molecular-mass polypeptides were analyzed in detail in photosystem II (PSII) complexes isolated from a thermophilic cyanobacterium, Thermosynechococcus vulcanus (formerly, Synechococcus vulcanus). PsbE, the large subunit polypeptide of cytochrome b(559), showed an apparent molecular mass much lower than the expected one. The unusually large mobility could be attributed to the large intrinsic net electronic charge. All other Coomassie-stained polypeptides were identified by N-terminal sequencing. In addition to the well-known cyanobacterial PSII polypeptides, such as PsbE, F, H, I, L, M, U, V and X, the presence of PsbY, PsbZ and Psb27 was also confirmed in the isolated PSII complexes. Furthermore, the whole amino acid sequence was determined for the polypeptide which was known as PsbN. The whole amino acid sequence revealed that this polypeptide was identical to PsbTc which has been found in higher plants and green algae. These results strongly suggest that PsbN is not a member of the PSII complex. It is also shown that cyanobacteria have cytochrome b(559) in the high potential form as in higher plants.

Amino Acid Sequence↗

PubMed2002

Temperature acclimation of photosynthesis and related changes in photosystem II electron transport in winter wheat.

Winter wheat (Triticum aestivum L. cv Norin No. 61) was grown at 25 degrees C until the third leaves reached about 10 cm in length and then at 15 degrees C, 25 degrees C, or 35 degrees C until full development of the third leaves (about 1 week at 25 degrees C, but 2-3 weeks at 15 degrees C or 35 degrees C). In the leaves developed at 15 degrees C, 25 degrees C, and 35 degrees C, the optimum temperature for CO(2)-saturated photosynthesis was 15 degrees C to 20 degrees C, 25 degrees C to 30 degrees C, and 35 degrees C, respectively. The photosystem II (PS II) electron transport, determined either polarographically with isolated thylakoids or by measuring the modulated chlorophyll a fluorescence in leaves, also showed the maximum rate near the temperature at which the leaves had developed. Maximum rates of CO(2)-saturated photosynthesis and PS II electron transport determined at respective optimum temperatures were the highest in the leaves developed at 25 degrees C and lowest in the leaves developed at 35 degrees C. So were the levels of chlorophyll, photosystem I and PS II, whereas the level of Rubisco decreased with increasing temperature at which the leaves had developed. Kinetic analyses of chlorophyll a fluorescence changes and P700 reduction showed that the temperature dependence of electron transport at the plastoquinone and water-oxidation sites was modulated by the temperature at which the leaves had developed. These results indicate that the major factor that contributes to thermal acclimation of photosynthesis in winter wheat is the plastic response of PS II electron transport to environmental temperature.

Acclimatization↗