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At least 1,009 records · Page 56Linked to original sources
PubMed2006

Evidence for involvement of photosynthetic processes in the stomatal response to CO2.

Stomatal conductance (gs) typically declines in response to increasing intercellular CO2 concentration (ci). However, the mechanisms underlying this response are not fully understood. Recent work suggests that stomatal responses to ci and red light (RL) are linked to photosynthetic electron transport. We investigated the role of photosynthetic electron transport in the stomatal response to ci in intact leaves of cocklebur (Xanthium strumarium) plants by examining the responses of gs and net CO2 assimilation rate to ci in light and darkness, in the presence and absence of the photosystem II inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU), and at 2% and 21% ambient oxygen. Our results indicate that (1) gs and assimilation rate decline concurrently and with similar spatial patterns in response to DCMU; (2) the response of gs to ci changes slope in concert with the transition from Rubisco- to electron transport-limited photosynthesis at various irradiances and oxygen concentrations; (3) the response of gs to ci is similar in darkness and in DCMU-treated leaves, whereas the response in light in non-DCMU-treated leaves is much larger and has a different shape; (4) the response of gs to ci is insensitive to oxygen in DCMU-treated leaves or in darkness; and (5) stomata respond normally to RL when ci is held constant, indicating the RL response does not require a reduction in ci by mesophyll photosynthesis. Together, these results suggest that part of the stomatal response to ci involves the balance between photosynthetic electron transport and carbon reduction either in the mesophyll or in guard cell chloroplasts.

Carbamide Peroxide↗
PubMed1999

The redox state regulates RNA degradation in the chloroplast of Chlamydomonas reinhardtii.

A Chlamydomonas reinhardtii chloroplast transformant, designated MU7, carrying a chimeric (rbcL promoter: beta-glucuronidase [GUS]: psaB 3' end) gene whose transcripts have been found previously to be unstable in light (half-life of 20 min in light as opposed to a half-life of 5 h in the dark), was used to study the role of electron transport and of the redox state in the degradation of chloroplast transcripts in the light. Blocking photosynthetic electron transport with 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) prevented the light-dependent breakdown of the pool of GUS transcripts in MU7 cells. Diamide, an oxidizing agent, caused a measurable delay in the degradation of GUS transcripts in the light. The addition of dithiothreitol (DTT), a dithiol reductant, to MU7 cells in which GUS transcript levels were stabilized by DCMU induced degradation of GUS transcripts. Similarly, DTT induced a decrease in the levels of GUS transcripts when added to MU7 cells in the dark period of the light/dark cycle, a period in which GUS transcript levels normally increase. The levels of transcripts of endogenous chloroplast genes were affected by DCMU and DTT in the same direction as levels of GUS transcripts. The results suggest a regulatory role of the redox state in the degradation of chloroplast transcripts in C. reinhardtii.

Animals↗
PubMed2001

Regulation of psbA and psaE expression by light quality in Synechocystis species PCC 6803. A redox control mechanism.

We investigated the influence of light of different wavelengths on the expression of the psbA gene, which encodes the D1 protein of the photosystem II and the psaE gene, which encodes the subunit Psa-E of the photosystem I, in Synechocystis sp PCC 6803. In an attempt to differentiate between a light-sensory and a redox-sensory signaling processes, the effect of orange, blue, and far-red light was studied in the wild-type and in a phycobilisome-less mutant. Transferring wild-type cells from one type of illumination to another induced changes in the redox state of the electron transport chain and in psbA and psaE expression. Blue and far-red lights (which are preferentially absorbed by the photosystem I) induced an accumulation of psbA transcripts and a decrease of the psaE mRNA level. In contrast, orange light (which is preferentially absorbed by the photosystem II) induced a large accumulation of psaE transcripts and a decrease of psbA mRNA level. Transferring mutant cells from blue to orange light (or vice versa) had no effect either on the redox state of the electron transport chain or on the levels of psbA and psaE mRNAs. Thus, light quality seems to regulate expression of these genes via a redox sensory mechanism in Synechocystis sp PCC 6803 cells. Our data suggest that the redox state of one of the electron carriers between the plastoquinone pool and the photosystem I has opposite influences on psbA and psaE expression. Its reduction induces accumulation of psaE transcripts, and its oxidation induces accumulation of psbA mRNAs.

Cyanobacteria↗
PubMed1997

Light-regulated changes in abundance and polyribosome association of ferredoxin mRNA are dependent on photosynthesis.

In transgenic tobacco plants containing a pea ferredoxin transcribed region (Fed-1) driven by the cauliflower mosaic virus 35S promoter (P35S), light acts at a post-transcriptional level to control the abundance of Fed-1 mRNA in green leaves. To determine whether the light signal for this response involves photosynthesis, we treated transgenic seedlings with or without 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU), an inhibitor of photosynthetic electron transport. DCMU prevented the normal light response by blocking reaccumulation of Fed-1 transcripts when dark-adapted green plants were returned to the light. In contrast, reaccumulation of light-harvesting complex B (Lhcb) transcripts was unaffected by DCMU treatment. Because Fed-1 light regulation requires translation, we also examined polyribosome profiles. We found that Fed-1 transcripts accumulated on polyribosomes in the light but were found primarily in non-polyribosomal fractions in dark-adapted plants or in illuminated plants exposed to lower than normal light intensity or treated with DCMU. Surprisingly, although Lhcb mRNA abundance was not affected by DCMU, its polyribosomal loading pattern was altered in much the same way as was that of Fed-1 mRNA. In contrast, DCMU had no effect on either the abundance or the polyribosome profiles of endogenous histone H1 or transgenic P35S::CAT transcripts. Thus, our results are consistent with the hypothesis that a process coupled to photosynthesis affects the polyribosome loading of a subset of cytoplasmic mRNAs.

Diuron↗
PubMed1993

Targeted interruption of the psaA and psaB genes encoding the reaction-centre proteins of photosystem I in the filamentous cyanobacterium Anabaena variabilis ATCC 29413.

The two reaction-centre proteins of the photosystem I (PSI) complex are encoded by two adjacent genes named psaA and psaB. We have performed targeted mutagenesis to insertionally inactivate each of these genes in the filamentous cyanobacterium Anabaena variabilis ATCC 29413. The resulting mutant strains, termed psaA::NmR and psaB::NmR, were blue because of a high ratio of phycobilin to chlorophyll and were unable to grow in light. These mutant cells also lacked chemically reducible P700 (the reaction-centre chlorophylls of PSI) and as a consequence did not exhibit any PSI-mediated photochemical activity. However, their photosystem II (PSII) complexes were fully active. The loss of the PsaA and PsaB proteins and their associated chlorophyll molecules resulted in a five- to sevenfold decrease in the chlorophyll/PSII ratio in the mutant cells relative to the wild-type cells. Interestingly, the psaB::NmR and not the psaA::NmR mutant strain retained a small fluorescence peak (77K) at 721 nm originating from chlorophyll molecule(s) presumably bound to a small amount of the PsaA protein present in the psaB mutant. These results demonstrate that this organism is suitable for the manipulation of PSI reaction-centre proteins.

Anabaena↗
PubMed2006

Phototropin involvement in the expression of genes encoding chlorophyll and carotenoid biosynthesis enzymes and LHC apoproteins in Chlamydomonas reinhardtii.

Phototropin (PHOT) is a photoreceptor involved in a variety of blue-light-elicited physiological processes including phototropism, chloroplast movement and stomatal opening in plants. The work presented here tests whether PHOT is involved in expression of light-regulated genes in Chlamydomonas reinhardtii. When C. reinhardtii was transferred from the dark to very low-fluence rate white light, there was a substantial increase in the level of transcripts encoding glutamate-1-semialdehyde aminotransferase (GSAT), phytoene desaturase (PDS) and light-harvesting polypeptides (e.g. LHCBM6). Increased levels of these transcripts were also elicited by low-intensity blue light, and this blue-light stimulation was suppressed in three different RNAi strains that synthesize low levels of PHOT. The levels of GSAT and LHCBM6 transcripts also increased following exposure of algal cells to low-intensity red light (RL). The red-light-dependent increase in transcript abundance was not affected by the electron transport inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea, implying that the influence of RL on transcript accumulation was not controlled by cytoplasmic redox conditions, and that a red-light photoreceptor(s) may be involved in regulating the levels of transcripts from specific photosynthesis-related genes in C. reinhardtii. Interestingly, elevated GSAT and LHCBM6 transcript levels in RL were significantly reduced in the PHOT RNAi strains, which raises the possibility of co-action between blue and RL signaling pathways. Microarray experiments indicated that the levels of several transcripts for photosystem (PS) I and II polypeptides were also modulated by PHOT. These data suggest that, in C. reinhardtii, (i) PHOT is involved in blue-light-mediated changes in transcript accumulation, (ii) synchronization of the synthesis of chlorophylls (Chl), carotenoids, Chl-binding proteins and other components of the photosynthetic apparatus is achieved, at least in part, through PHOT-mediated signaling, and (iii) a red-light photoreceptor can also influence levels of certain transcripts associated with photosynthetic function, although its action requires normal levels of PHOT.

Algal Proteins↗
PubMed1975

Diaminobenzidine an electron donor to photosystem 1 and to photosystem 2 in chloroplasts.

1. 3,3'-Diaminobenzidine was shown to serve as an electron donor to photosystem 1 in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea. In Tris-treated chloroplasts diaminobenzidine serves as an electron donor to photosystem 1 and to photosystem 2; the latter is sensitive to 3-(3,4-dichlorophenyl)-1,1-dimethylurea. 2. Addition of diaminobenzidine to Tris-treated chloroplasts causes an increase in fluorescence yield. 3. Diaminobenzidine-dependent electron transport mediated by photosystem 2 is coupled to synthesis of ATP even in the absence of an electron acceptor. This phosphorylation which is presumably supported by cyclic electron flow, is sensitive to 3-(3,4-dichlorophenyl)-1,1-dimethylurea. 4. Diaminobenzidine-dependent ATP formation, in Tris-treated chloroplasts exhibits the red-drop phenomenon. 5. The diaminobenzidine-induced cyclic photophosphorylation (mediated by photosystem 2) is resistant to a large extent to KCN-treatment which is known to inhibit reactions catalyzed by photosystem 1. On the other hand ATP formation supported by electron transport from diaminobenzidine to methyl viologen [in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea] is largely inhibited by KCN-treatment. This observation suggests that there are two coupling sites of ATP formation, one catalyzed by diaminobenzidine as a donor to photosystem 1 (in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea), and the other supported by diaminobenzidine which acts both as a donor to photosystem 2 (in Tris-treated chloroplasts) and as an acceptor (in its oxidized form) from a carrier located between the two photosystems.

3,3'-Diaminobenzidine↗
PubMed1976

Torpedo marmorata acetylcholinesterase; a comparison with the Electrophorus electricus enzyme. Molecular forms, subunits, electron microscopy, immunological relationship.

Electron microscopy, sequential degradation by hydrolytic enzymes and the physical-chemical properties of the molecular forms of Torpedo acetylcholinesterase indicate that these molecules are structurally related to each other in the same way as the molecular forms of Electrophorus acetylcholinesterase: all are derived from a complex structure in which three tetrameric groups of subunits are associated with a rod-like 'tail'. In aged preparations the catalytic subunits are split into fragments in a manner similar to those of Electrophorus acetylcholinesterase. Immunological cross-reaction between both enzymes demonstrates the occurrence of common antigenic sites. The enzymes from the two sources, however, are different in their molecular weights and susceptibility to hydrolytic enzymes. Also, Torpedo acetylcholinesterase does not precipitate with either isologous or heterologous antibodies.

Acetylcholinesterase↗
PubMed1976

Molecular forms of Electrophorus acetylcholinesterase. Molecular weight and composition.

Molecular weights for the series of six Electrophorus acetylcholinesterase forms have been determined either by the sedimentation-diffusion equilibrium method or, particularly in the case of the very scarce G' and G inches forms, from their Stokes radius and sedimentation coefficient values. Both methods are in excellent agreement. The results provide good evidence for the model previously proposed, G inches, G' and G containing one, two and four subunits, whereas A, C and D possess, in addition to respectively one, two and three tetrameric sets of such subunits, a structural element, the tail. Although the amino acid composition of 'tailed' and globular forms did not reveal any significant feature of this element, its mass, about 100 000 daltons, could be deduced from a comparison of molecular weights for the two classes of acetylcholinesterase forms. This value is in close agreement with electron microscopic data. The tail is thought to consist of three 30 000-dalton strands.

Acetylcholinesterase↗
PubMed1979

Photoreactions of cytochrome b563 and f554 in intact spinach chloroplasts: regulation of cyclic electron flow.

In intact spinach chloroplasts cytochrome b563 and cytochrome f show an antagonistic redox behaviour in the extent and kinetics of light/dark-induced absorbance changes. The extent of cytochrome b563 photoreduction appears to be influenced by the redox state of plastoquinone suggesting a regulation of cyclic electron flow at this level. Far-red illumination induces a membrane state with altered redox reactions of both cytochromes at a more oxidized level.

Chloroplasts↗
PubMed1980

Chloroplast phosphoproteins. Evidence for a thylakoid-bound phosphoprotein phosphatase.

1. Isolated intact pea (Pisum sativum) chloroplasts incorporate [32P]orthophosphate into several thylakoid polypeptides in the light. Transfer of the labelled chloroplasts to darkness results in rapid dephosphorylation of the polypeptides. The most rapidly dephosphorylated phosphoproteins are the 26000-Mr doublet derived from the light-harvesting chlorophyll a/b binding complex. 2. Incubation of isolated 32P-labelled thylakoids in buffer in the absence of stromal components also results in rapid protein dephosphorylation. Again, the most rapidly dephosphorylated phosphoproteins are the 26000-Mr light-harvesting doublet. Dephosphorylation of all thylakoid phosphoproteins is accelerated by addition of up to 10 mM MgCl2. 3. The enzyme responsible for dephosphorylation is a phosphatase rather than a phosphotransferase or the thylakoid protein kinase acting in reverse. The enzyme is specifically and totally inhibited by NaF and does not require phosphoryl group acceptors such as ADP. Unlike the protein kinase, the phosphatase is indifferent to light and the electron transport inhibitor 3(3,4-dichlorophenyl)-1,1-dimethylurea. 4. The phosphorylated regions of the thylakoid phosphoproteins protrude from the outer surface of the membrane and are removed by trypsin treatment.

Chloroplasts↗
PubMed1980

Photoreactions of cytochromes in algal chloroplasts.

Light-induced cytochrome redox reactions were investigated with algal chloroplasts capable of high rates of electron transport coupled to phosphorylation. The electron-donor pool preceding photosystem I consists of membrane-bound cytochrome f-554.5 and a soluble cytochrome c-553; the latter replaces the function of plastocyanin of higher-plant chloroplasts. Both cytochromes are reduced by photosystem II and oxidized by photosystem I. A site of energy conservation precedes these c-type cytochromes. The data obtained with respect to the function of b-type cytochromes are comparable to those obtained with higher-plant chloroplasts. Cyclic electron transport is mediated by cytochrome b-563 in a photosystem-I-dependent reaction. In addition, cytochrome b-563 may be reduced by photosystem II, in accordance with recent findings with intact spinach chloroplasts. It therefore appears that cytochrome b-563 is a member of both cyclic and non-cyclic electron transport. In contrast to higher-plant chloroplasts, redox reactions of cytochrome b-559 are observable without any pretreatments. Cytochrome b-559, high-potential, is reduced by photosystem II through plastoquinone. In the presence of carbonyl cyanide m-chlorophenylhydrazone a cytochrome-b-559 oxidation by photosystem II is measured.

Carbonyl Cyanide m-Chlorophenyl Hydrazone↗
PubMed1991

Inorganic-pyrophosphate-dependent phosphorylation of spinach thylakoid proteins.

It has been shown for the first time that several photosystem-II thylakoid proteins and the main chlorophyll-a/b light-harvesting complex can be phosphorylated with inorganic pyrophosphate as phosphate donor. With pyrophosphate, as with ATP, the protein-kinase reaction is dependent on light or a strong reducing agent. The reaction which can be demonstrated in well-washed spinach thylakoids is dependent on electron transport and is controlled by the redox state of the plastoquinone pool. It is suggested that the pyrophosphate-dependent thylakoid protein phosphorylation is mediated by the same kinase which is responsible for the ATP-dependent protein phosphorylation. This pyrophosphate-dependent kinase activity may be derived from an evolutionary precursor from which ATP-dependent protein phosphorylation also developed.

Adenosine Triphosphate↗