SEARCH · Search PubMed

Results for “Diuron”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 991 records · Page 55Linked to original sources

PubMed1998

The herbicide-resistant species of the cyanobacterial D1 protein obtained by thorough and random in vitro mutagenesis.

Random mutations were introduced into the DNA fragment of the psbA2 gene of Synechocystis sp. PCC 6803, which encodes the carboxyl-terminal 178 amino acid region of the D1 protein of the PSII reaction center, by in vitro random mutagenesis to obtain D1 species resistant to herbicides and to understand the protein-herbicide interactions. The mutants were screened on the criterion of resistance to either 1 microM DCMU or 10 microM atrazine. In these mutants, amino acid substitutions were distributed throughout the entire area of the targeted region in the D1 protein. However, in every mutant, except for one case, the substitution was present in the region described as the "herbicide-binding niche", i.e., between Phe211 and Leu275, although some amino acid substitutions which were not previously described were found at residues known to be involved with herbicide affinity. Thus, the result of random mutagenesis basically supports the validity of the proposed structural model for the D1 protein, as well as of the herbicide-binding niche. Preliminary characterization of the herbicide-resistant mutants obtained in this study has also been conducted.

Amino Acid Sequence↗

PubMed2000

Photosynthetic acclimation of the filamentous cyanobacterium, Plectonema boryanum UTEX 485, to temperature and light.

Photosynthetic acclimation to temperature and irradiance was studied in the filamentous, non-heterocystous cyanobacterium Plectonema boryanum UTEX 485. Growth rates of this cyanobacterium measured at ambient CO2 were primarily influenced by temperature with minimal effects of irradiance. Both growth temperature and irradiance affected linolenic (18:3) and linoleic acid (18:2) levels in the four major lipid classes in an independent but additive manner. In contrast, photosynthetic acclimation was not due to either growth temperature or irradiance per se, but rather, due to the interaction of these environmental factors. P. boryanum grown at low temperature and moderate irradiance mimicked cells grown at high light. Compared to cells grown at either 29 degrees C/150 micromol m(-2) s(-1) (29/150) or 15/10, P. boryanum grown at either 15/150 or 29/750 exhibited: (1) reduced cellular levels of Chl a and phycobilisomes (PBS), and concomitantly higher content of an orange-red carotenoid, myxoxanthophyll; (2) higher light saturated rates (Pmax) when expressed on a Chl a basis but lower apparent quantum yields of oxygen evolution and (3) enhanced resistance to high light stress. P. boryanum grown at 15/150 regained normal blue-green pigmentation within 16 h after a temperature shift to 29 degrees C at a constant irradiance of 150 micromol m(-2) s(-1). DBMIB and KCN but not DCMU and atrazine partially inhibited the change in myxoxanthophyll/Chl a ratio following the shift from 15 to 29 degrees C. We conclude that P. boryanum responds to either varying growth temperature or varying growth irradiance by adjusting the ability to absorb light through decreasing the cellular contents of Chl a and light-harvesting pigments and screening of excessive light by myxoxanthophyll predominantly localized in the cell wall/cell membrane to protect PSII from over-excitation. The possible role of redox sensing/signalling for photosynthetic acclimation of cyanobacteria to either temperature or irradiance is discussed.

Acclimatization↗

PubMed2000

Photosynthetic electron flow regulates transcription of the psaB gene in pea (Pisum sativum L.) chloroplasts through the redox state of the plastoquinone pool.

Plants respond to changing light conditions by altering the stoichiometry between components of the photosynthetic electron transport chain of chloroplast thylakoids. We measured specific run-on transcription of the chloroplast genes psaB, psbA and rbcL in pea (Pisum sativum L.) seedlings grown under three different conditions of illumination: light selective for photosystem I (PSI-light); light selective for photosystem II (PSII-light); and a combination of PSI- and PSII-light (mixed light, ML). The transcriptional rate of the psaB gene increased under PSII-light and decreased under PSI-light, while the transcriptional rates of the psbA and rbcL genes were affected only in a non-specific way. Similar effects also occurred in plants grown under ML and switched to either PSI- or PSII-light for 4 h. Addition of the inhibitors of photosynthetic electron transport 3-(3,4 dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB) influenced psaB transcription in isolated, illuminated chloroplasts: DCMU addition resulted in oxidation of the plastoquinone pool and decreased transcription of psaB; DBMIB addition resulted in reduction of the plastoquinone pool and increased transcription of psaB. The experimental results obtained in vivo and in vitro provide evidence for coupling between the redox state of plastoquinone and the rate of transcription of the psaB gene in pea.

Chloroplasts↗

PubMed2001

Physiological significance of the regulation of photosystem stoichiometry upon high light acclimation of Synechocystis sp. PCC 6803.

We characterized the photosynthetic properties of the pmgA mutant of Synechocystis PCC 6803, which cannot change its photosystem stoichiometry under a high-light condition (200 micromol x m(-2) x s(-1)), in order to clarify the physiological significance of the regulation of photosystem stoichiometry. We found that (1) PSII activity was inhibited more in wild-type cells on the first day under the high-light conditions than in mutant cells. (2) The growth of the mutants following the initial imposition of high light was faster than that of wild-type cells. (3) However, growth was severely inhibited in the mutants after the third day of exposure to high light. (4) The growth inhibition in the mutants under the extended high-light conditions was reversed by the addition of sublethal concentrations of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU), which seemed to mimic photoinhibition of PSII. These results suggest that the main role of adjusting the photosystem stoichiometry with respect to light intensity is not to maintain efficient photosynthesis, but to down regulate electron transfer. Failure to down regulate electron flow leads to cell death under prolonged exposure to high light in this cyanobacterium.

Cyanobacteria↗

PubMed2001

Guard-cell chloroplasts provide ATP required for H(+) pumping in the plasma membrane and stomatal opening.

To elucidate the role of guard-cell chloroplasts (GCCs) in stomatal movement, we investigated the effects of oligomycin, an inhibitor of oxidative phosphorylation, and 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU), an inhibitor of photosystem II, on fusicoccin (FC)-induced H(+) pumping and stomatal opening. FC was found to induce H(+ )pumping in guard-cell protoplasts (GCPs) from Vicia faba and stomatal opening in the epidermis of Commelina benghalensis; and, red light (RL) slightly stimulated these responses. Oligomycin strongly inhibited the pumping and stomatal opening in the dark. RL partially reversed the inhibitions, and DCMU decreased the effect of RL. FC activated the plasma membrane H(+)-ATPase (EC 3.6.1.35) in GCPs similarly irrespective of these treatments, indicating that the H(+)-ATPase activity was not the limiting step in H(+) pumping. Oligomycin significantly decreased the ATP content in GCPs in the dark. RL partially reversed this effect, and DCMU eliminated the effect of RL. A significant part of the ATP produced by photophosphorylation to H(+) pumping was indicated under RL. These results suggest that GCCs supply ATP to the cytosol under RL, and that the ATP is utilized by the plasma membrane H(+)-ATPase for H(+) pumping.

Cell Membrane↗

PubMed2002

Nitric oxide production mediated by nitrate reductase in the green alga Chlamydomonas reinhardtii: an alternative NO production pathway in photosynthetic organisms.

Biological activity of nitric oxide (NO) production was investigated in the unicellular green alga Chlamydomonas reinhardtii. An NO specific electrode detected a rapid increase in signal when nitrite (NO(2)(-)) was added into a suspension of C. reinhardtii intact cells in the dark. The addition of KCN or the NO quencher bovine hemoglobin completely abolished the signal, verifying that the nitrite-dependent increase in signal is due to enzymatic NO production. L-arginine, the substrate for NO synthase, did not induce detectable NO production and the NOS inhibitor N(omega)-nitro-L-arginine showed no inhibitory effect on the nitrite-dependent production of NO. Illuminating cells showed a significant suppressive effect on NO production. When the photosynthetic electron transport inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea was present in the suspension, C. reinhardtii cells produced NO after the addition of nitrite even under illumination. Kinetic and microscopic observations, using the intracellular fluorescent NO probe 4,5-diaminofluorescein-2 diacetate, both demonstrated that NO was produced within the cells in response to the addition of nitrite. The Chlamydomonas mutant cc-2929, which lacks nitrate reductase (NR) activity, did not display any of the responses observed in the wild-type cells. The results presented here provide direct in vivo evidence to confirm that NR is involved in the nitrite-dependent NO production in the green alga.

Animals↗

PubMed2002

Photosynthetic electron transport regulates the stability of the transcript for the protochlorophyllide oxidoreductase gene in the liverwort, Marchantia paleacea var. diptera.

The transfer of Marchantia paleacea var. diptera cells to darkness caused a reversible repression in the accumulation of transcript for a gene, por, encoding the NADPH: protochlorophyllide oxidoreductase (EC 1.3.1.33). The photosynthetic inhibitor DCMU and DBMIB repressed the accumulation in light. In the presence of transcription inhibitor cordycepin, not only incubation in the dark but also addition of DCMU or DBMIB in light stimulated the degradation of the por transcript. These findings suggest that photosynthetic electron transport is involved in regulating the stability of the por transcript.

Darkness↗

PubMed2002

Dual roles of photosynthetic electron transport in photosystem I biogenesis: light induction of mRNAs and chromatic regulation at post-mRNA level.

Light regulation of photosystem I (PSI) biogenesis was studied in a unicellular green alga, Chlamydomonas reinhardtii. When Chlamydomonas cells were transferred from darkness to the light, mRNAs for both nuclear- and chloroplast-encoded PSI subunits were induced in concert. This light induction was inhibited by photosynthetic electron transport (PET) inhibitors, 3-(3,4 dichlorophenyl)-1,1-dimethylurea and 2,5-dibromo-3-methyl-6 isopropyl-p-benzoquinone, but not by an uncoupler, carbonyl cyanide m-chlorophenylhydrazone. This indicated that PET plays a pivotal role in the light induction of PSI subunit mRNAs, but that photophosphorylation is not necessary. When we irradiated the Chlamydomonas cells with PSI-light (695 nm) or PSII-light (644 nm), which makes the plastoquinone pool oxidative and reductive, respectively, PSII-light caused the accumulation of PSI proteins more abundantly than did PSI-light. However, there was no difference for the PSI subunit mRNA levels between these light sources. From these results, we conclude that PET plays dual roles in the regulation of PSI biogenesis in Chlamydomonas: when cells are illuminated, PET first induces the PSI subunit mRNAs irrespective of the redox state of the intersystem electron carriers, and then their redox state fine-tunes PSI biogenesis at translational and/or post-translational steps to fulfil the chromatic adaptation.

Animals↗

PubMed2003

Binding and functional properties of the extrinsic proteins in oxygen-evolving photosystem II particle from a green alga, Chlamydomonas reinhardtii having his-tagged CP47.

Oxygen-evolving photosystem II (PSII) particles were purified from Chlamydomonas reinhardtii having His-tag extension at the C terminus of the CP47 protein, by a single-step Ni(2+)-affinity column chromatography after solubilization of thylakoid membranes with sucrose monolaurate. The PSII particles consisted of, in addition to intrinsic proteins, three extrinsic proteins of 33, 23 and 17 kDa. The preparation showed a high oxygen-evolving activity of 2,300-2,500 micro mol O(2) (mg Chl)(-1) h(-1) in the presence of Ca(2+) using ferricyanide as the electron acceptor, while its activity was 680-720 micro mol O(2) (mg Chl)(-1) h(-1) in the absence of Ca(2+) and Cl(-) ions. The activity was 710-820 micro mol O(2) (mg Chl)(-1) h(-1) independent of the presence or absence of Ca(2+) and Cl(-) when 2,6-dichloro-p-benzoquinone was used as the acceptor. These activities were scarcely inhibited by DCMU. The kinetics of flash-induced fluorescence decay revealed that the electron transfer from Q(A)(-) to Q(B) was significantly inhibited, and the electron transfer from Q(A)(-) to ferricyanide was largely stimulated in the presence of Ca(2+). These results indicate that the acceptor side, Q(B) site, was altered in the PSII particles but its donor side remained intact. Release-reconstitution experiments revealed that the extrinsic 23 and 17 kDa proteins were released only partially by NaCl-wash, while most of the three extrinsic proteins were removed when treated with urea/NaCl, alkaline Tris or CaCl(2). The 23 and 17 kDa proteins directly bound to PSII independent of the other extrinsic proteins, and the 33 kDa protein functionally re-bound to CaCl(2)-treated PSII which had been reconstituted with the 23 and 17 kDa proteins. These binding properties were largely different from those of the extrinsic proteins in higher plant PSII, and suggest that each of the three extrinsic proteins has their own binding sites independent of the others in the green algal PSII.

Algal Proteins↗

PubMed2003

Effects of low CO2 on NAD(P)H dehydrogenase, a mediator of cyclic electron transport around photosystem I in the cyanobacterium synechocystis PCC6803.

The expression and activity of type-1 NAD(P)H dehydrogenase (NDH-1) was compared between cells of Synechocystis PCC6803 grown in high (H-cells) and low (L-cells) CO(2) conditions. Western analysis indicated that L-cells contain higher amounts of the NDH-1 subunits, NdhH, NdhI and NdhK. An NADPH-specific subcomplex of NDH-1 showed higher NADPH-nitroblue tetrazolium oxidoreductase activity in L-cells. The activities of both NADPH-menadione oxidoreductase and light-dependent NADPH oxidation driven by photosystem I were much higher in L-cells than in H-cells. The initial rate of re-reduction of P700(+) following actinic light illumination in the presence of DCMU under background far-red light was enhanced in L-cells. In addition, rotenone, a specific inhibitor of NDH-1, suppressed the relative rate of post-illumination increase in Chl fluorescence of L-cells more than that of H-cells, suggesting that the involvement of NDH-1 in cyclic electron flow around photosystem I was enhanced by low CO(2). Taken together, these results suggest that NDH-1 complex and NDH-1-mediated cyclic electron transport are stimulated by low CO(2) and function in the acclimation of cyanobacteria to low CO(2).

Blotting, Western↗

PubMed2003

Redox changes in the chloroplast and hydrogen peroxide are essential for regulation of C(3)-CAM transition and photooxidative stress responses in the facultative CAM plant Mesembryanthemum crystallinum L.

Mesembryanthemum crystallinum, a facultative halophyte and C(3)-Crassulacean acid metabolism (CAM) intermediate plant, has become a favoured plant for studying stress response mechanisms during C(3)-CAM shifts. One hour of exposure to excess light (EL) caused inhibition of photosynthetic electron transport in M. crystallinum leaves as indicated by chlorophyll a fluorescence measurements. This was accompanied by an increase in NADP-malic enzyme (ME), one of the key cytosolic enzymes involved in CAM, and by a general increase in superoxide dismutase (SOD) activity. In contrast, NAD-ME activity (the mitochondrial form of ME) was not affected by EL. Exposure to EL and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB) treatment of a whole plant in low light induced hydrogen peroxide (H(2)O(2)) and C(3) to CAM transition. In contrast, treatment with 3-3,4-dichlorophenyl-1,1-dimethyl urea (DCMU) has blocked high light-induced H(2)O(2) accumulation and C(3)-CAM transition. Moreover, the abundance of transcripts encoding different SODs, ascorbate peroxidase and SOD activity was differently regulated by DCMU and DBMIB. Results of applying EL or high light, H(2)O(2) and photosynthetic electron transport inhibitors suggest that the redox events in the vicinity of PSII and/or PSI and photo-produced H(2)O(2) play a major role in the regulation of C(3)-CAM transition and photooxidative stress responses in M. crystallinum.

Chloroplasts↗

PubMed2004

Photosynthetic electron transport differentially regulates the expression of superoxide dismutase genes in liverwort, Marchantia paleacea var. diptera.

Liverwort, Marchantia paleacea var. diptera, contains Mn-superoxide dismutase (Mn-SOD) in mitochondria, Fe-SOD in chloroplast and CuZn-SOD in cytosol. An Mn-SOD gene (MpMnSOD) was isolated from the liverwort. Using this clone together with the liverwort Fe-SOD and CuZn-SOD genes as probes, the expression of three SOD genes was investigated. Under heterotrophic conditions, the transcript of three SOD genes was accumulated light independently. On the other hand, under photoautotrophic conditions, the transcript levels of Fe-SOD and Mn-SOD increased in the light while that of CuZn-SOD decreased. The reverse occurred in the dark. In contrast to the transcript level, the activity of the three SODs was barely affected by light. The transcription inhibitor, cordycepin, inhibited either the light-promoted accumulation of Fe-SOD and Mn-SOD transcript or the light-induced reduction of the CuZn-SOD transcript. Photosynthetic electron transport inhibitors, DCMU and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone, inhibited the photo-response in three SOD genes. These results suggest that the transcript abundance of three SOD genes in liverwort is regulated by photosynthetic electron transport but the mechanism regulating the transcript abundance of the CuZn-SOD gene is different from that of the Fe-SOD and Mn-SOD genes.

Amino Acid Sequence↗

PubMed2004

Photosynthetic electron transport controls expression of the high light inducible gene in the cyanobacterium Synechococcus elongatus strain PCC 7942.

The hliA gene of Synechococcus, encoding a photoprotective high light inducible polypeptide, is up-regulated by high light (HL) or low intensity blue/UV-A light (BL). hliA expression was found to be up-regulated by KCN in low light (LL) (but not in the dark), and up-regulation in HL, BL, and LL (with KCN) was inhibited by 2,5-dibromo-3-methyl-6-isopropyl-benzoquinone. A working hypothesis is proposed whereby up-regulation is in response to the reduced state of cytochrome b(6)f or a carrier beyond in photosynthesis. Modest up-regulation occurs in LL by treatment with 3-(3,4-dichlorophenyl)-1,1-dimethylurea, but this is related to effects on hliA mRNA stability rather than on transcription.

Bacterial Proteins↗

PubMed2002

Mitochondrial-driven bicarbonate transport supports photosynthesis in a marine microalga.

The CO(2)-concentrating mechanism (CCM) of the marine eustigmatophycean microalga Nannochloropsis gaditana consists of an active HCO(3)(-) transport system and an internal carbonic anhydrase to facilitate accumulation and conversion of HCO(3)(-) to CO(2) for photosynthetic fixation. Aqueous inlet mass spectrometry revealed that a portion of the CO(2) generated within the cells leaked to the medium, resulting in a significant rise in the extracellular CO(2) concentration to a level above its chemical equilibrium that was diagnostic for active HCO(3)(-) transport. The transient rise in extracellular CO(2) occurred in the light and the dark and was resolved from concurrent respiratory CO(2) efflux using H(13)CO(3)(-) stable isotope techniques. H(13)CO(3)(-) pump-(13)CO(2) leak activity of the CCM was unaffected by 10 microM 3(3,4-dichlorophenyl)-1,1-dimethylurea, an inhibitor of chloroplast linear electron transport, although photosynthetic O(2) evolution was reduced by 90%. However, low concentrations of cyanide, azide, and rotenone along with anoxia significantly reduced or abolished (13)CO(2) efflux in the dark and light. These results indicate that H(13)CO(3)(-) transport was supported by mitochondrial energy production in contrast to other algae and cyanobacteria in which it is supported by photosynthetic electron transport. This is the first report of a direct role for mitochondria in the energization and functioning of the CCM in a photosynthetic organism.

Azides↗

PubMed2002

Light-intensity-dependent expression of Lhc gene family encoding light-harvesting chlorophyll-a/b proteins of photosystem II in Chlamydomonas reinhardtii.

Excessive light conditions repressed the levels of mRNAs accumulation of multiple Lhc genes encoding light-harvesting chlorophyll-a/b (LHC) proteins of photosystem (PS)II in the unicellular green alga, Chlamydomonas reinhardtii. The light intensity required for the repression tended to decrease with lowering temperature or CO(2) concentration. The responses of six LhcII genes encoding the major LHC (LHCII) proteins and two genes (Lhcb4 and Lhcb5) encoding the minor LHC proteins of PSII (CP29 and CP26) were similar. The results indicate that the expression of these Lhc genes is coordinately repressed when the energy input through the antenna systems exceeds the requirement for CO(2) assimilation. The Lhc mRNA level repressed under high-light conditions was partially recovered by adding the electron transport inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea, suggesting that redox signaling via photosynthetic electron carriers is involved in the gene regulation. However, the mRNA level was still considerably lower under high-light than under low-light conditions even in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Repression of the Lhc genes by high light was prominent even in the mutants deficient in the reaction center(s) of PSII or both PSI and PSII. The results indicate that two alternative processes are involved in the repression of Lhc genes under high-light conditions, one of which is independent of the photosynthetic reaction centers and electron transport events.

Algal Proteins↗

PubMed1993

Phytochrome levels in the green alga Mesotaenium caldariorum are light regulated.

Experiments undertaken in this investigation examine the influence of light on the levels of phytochrome in the green alga Mesotaenium caldariorum and also provide partial protein sequence of the algal phytochrome. Immunochemical and spectrophotometric measurements reveal that phytochrome levels increase nearly 4-fold upon transfer of light-grown algal cells to total darkness during a 6- to 8-d adaptation period. Within 24 h after return to continuous illumination, the level of phytochrome in dark-adapted cells has decreased to that found in light-grown cells. Red or far-red light experiments show that both effects of light, phytochrome accumulation during dark adaptation and light-dependent decrease of phytochrome, do not depend on the form of the phytochrome photoreceptor (i.e. far-red absorbing or red absorbing) present in the algal cell. The light-dependent reduction of phytochrome in dark-adapted cells is inhibited by the photosynthetic electron transport inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethyl urea, suggesting that this light effect is mediated by photosynthesis. Microsequence analyses of internal peptides indicate that algal phytochrome purified from dark-adapted cells shares the greatest sequence identity with phytochrome from the fern Selaginella (74%). Compared with higher plant photoreceptors, Mesotaenium phytochrome appears to be more closely related to phyB gene products (i.e. 62 and 63% average sequence identity) than to phyA gene products (i.e. 50 and 53% average sequence identity). Because light regulation and the structure of Mesotaenium phytochrome do not conform with either type I (light-labile) or type II (light-stable) phytochromes from higher plants, these results support the hypothesis that the lower green plant photoreceptors represent a distinct class of phytochrome.

Adaptation, Biological↗

PubMed1993

Dark heterotrophic growth conditions result in an increase in the content of photosystem II units in the filamentous cyanobacterium Anabaena variabilis ATCC 29413.

The filamentous nitrogen-fixing cyanobacterium Anabaena variabilis ATCC 29413 is capable of heterotrophic growth in complete darkness. After 6 months of continuous dark growth, both the autotrophic and heterotrophic cultures were found to have the same doubling time of 14 h. On a cellular basis, the chlorophyll content remained the same and the phycobilin content showed an increase in the dark-grown cultures. Fluorescence emission spectra at 77 K of dark-grown cells indicated that the phycobilisomes are functionally associated with photosystem II (PSII). Moreover, upon transfer to light, the dark-grown cells readily evolved oxygen. Although photosystem I (PSI) and whole chain-mediated electron transfer rates were comparable in both types of cultures, the rate of PSII-mediated electron transfer was found to be 20% higher in dark-grown cells. The PSI to PSII ratio changed from 6:1 in autotrophic cultures to 4:1 in the dark-grown cells. These changes in the rate of PSII electron transfer and in the stoichiometry between the two photosystems under dark, heterotrophic growth conditions were brought about by a preferential increase in the number of PSII units while the number of PSI units remained unchanged. The advantages of using this organism in the selection of PSI-deficient mutants are discussed.

Anabaena↗

PubMed2004

Activation of photosynthesis and resistance to photoinhibition in cyanobacteria within biological desert crust.

Filamentous cyanobacteria are the main primary producers in biological desert sand crusts. The cells are exposed to extreme environmental conditions including temperature, light, and diurnal desiccation/rehydration cycles. We have studied the kinetics of activation of photosynthesis during rehydration of the cyanobacteria, primarily Microcoleus sp., within crust samples collected in the Negev desert, Israel. We also investigated their susceptibility to photoinhibition. Activation of the photosynthetic apparatus, measured by fluorescence kinetics, thermoluminescence, and low temperature fluorescence emission spectra, did not require de novo protein synthesis. Over 50% of the photosystem II (PSII) activity, assembled phycobilisomes, and photosystem I (PSI) antennae were detected within less than 5 min of rehydration. Energy transfer to PSII and PSI by the respective antennae was fully established within 10 to 20 min of rehydration. The activation of a fraction of PSII population (about 20%-30%) was light and temperature-dependent but did not require electron flow to plastoquinone [was not inhibited by 3-(3,4-dichlorophenyl)-1,1-dimethylurea]. The cyanobacteria within the crusts are remarkably resistant to photoinhibition even in the absence of protein synthesis. The rate of PSII repair increased with light intensity and with time of exposure. Consequently, the extent of photoinhibition in high-light-exposed crusts reached a constant, relatively low, level. This is in contrast to model organisms such as Synechocystis sp. strain PCC 6803 where PSII activity declined continuously over the entire exposure to high illumination. Ability of the crust's organisms to rapidly activate photosynthesis upon rehydration and withstand photoinhibition under high light intensity may partly explain their ability to survive in this ecosystem.

Adaptation, Physiological↗