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Query: UMLS:C1832526 (PCC)
 5,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cyanobacteria respond to nutrient stress conditions by degrading their light-harvesting complexes for photosynthesis, a process regulated in Synechococcus sp. PCC 7942 by the sensor histidine kinase non-bleaching sensor (NblS). In yeast two-hybrid screenings for proteins interacting with NblS we have identified a novel type of protein, named SipA for NblS interacting protein A. Specific binding between NblS and SipA is observed with both yeast and bacterial two-hybrid systems. Additional yeast two-hybrid screenings with SipA as bait further confirmed the specificity of the interaction and allowed us to map their determinants to the ATP-binding domain of NblS. Strong conservation and coevolution of both NblS and SipA in cyanobacteria further suggests the importance of SipA in the context of the NblS signal transduction network.
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PMID:SipA, a novel type of protein from Synechococcus sp. PCC 7942, binds to the kinase domain of NblS. 1645 Nov 77

A Synechocystis sp. strain PCC 6803 mutant lacking CtaI, a main subunit of cytochrome c oxidase, is not capable of growing at light intensities below 5 micromol photons m(-2) s(-1), presumably due to an overreduced plastoquinone pool in the thylakoid membrane. Upon selection for growth at light intensities below 5 micromol photons m(-2) s(-1), a secondary mutant was generated that retained the CtaI deletion and had fully assembled photosystem II complexes; in this secondary mutant (pseudorevertant), oxygen evolution and respiratory activities were similar to those in the wild type. Functional complementation of the original CtaI-less strain to low-light tolerance by transformation with restriction fragments of genomic DNA of the pseudorevertant and subsequent mapping of the pseudoreversion site showed that the point mutation led to a Ser186Cys substitution in Sll1717, a protein of as-yet-unknown function and with a predicted ATP/GTP-binding domain. This mutation caused a decrease in the plastoquinone pool reduction level of thylakoids compared to that observed for the wild type. Based on a variety of experimental evidence, the most plausible mechanism to cause this effect is an activation of plastoquinol oxidation in thylakoids by the quinol oxidase CydAB that occurs without upregulation of the corresponding gene and that may be caused by an increased CydAB activity in thylakoids, conceivably due to altered CydAB sorting between cytoplasmic and thylakoid membranes. Sll1717 appears to be unique to Synechocystis sp. strain PCC 6803 and has a close homologue encoded in the genome of this organism. The transcript level of sll1717 is low, which suggests that the corresponding protein is regulatory rather than structural.
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PMID:Sll1717 affects the redox state of the plastoquinone pool by modulating quinol oxidase activity in thylakoids. 1645 10

Prochlorococcus is one of the most important primary producers on Earth; its unusual features and ecological importance have made it a model organism, but nutrient assimilation has received little attention. Glutamine synthetase (GS) plays a key role in nitrogen metabolism and its central position justifies the fine regulation of this enzyme. The aim of this work is to demonstrate the involvement of metal-catalyzed oxidation (MCO) in the control of the biological activity and turnover of GS from Prochlorococcus. In order to study the physiological role of MCO, we have first characterized the in vitro biosynthetic inactivation and degradation of GS in the axenic PCC 9511 strain, testing then the effect of several stress conditions, such as the presence of electron transport inhibitors, darkness and aging, on the inactivation and degradation of GS. It is noteworthy that the physiological substrates of GS could protect the enzyme from the oxidative inactivation and ATP partially reverted this inactivation once the enzyme had been oxidized, being this effect higher in the presence of glutamate. We have also found that the GS from aged cultures is degraded to the same smaller size fragments obtained in the in vitro degradation of GS by an oxidative model system (Fe3+/NADH/NADH oxidase/O2). These results suggest the implication of MCO in the age- and oxidative state-dependent degradation of GS from Prochlorococcus.
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PMID:Glutamine synthetase degradation is controlled by oxidative proteolysis in the marine cyanobacterium Prochlorococcus marinus strain PCC 9511. 1653 Mar 32

Photosystem I contains several peripheral membrane proteins that are located on either positive (luminal) or negative (stromal or cytoplasmic) sides of thylakoid membranes of chloroplasts or cyanobacteria. Incorporation of two peripheral subunits into photosystem I of the cyanobacterium Synechocystis species PCC 6803 was studied using a reconstitution system in which radiolabeled subunits II (PsaD) and IV (PsaE) were synthesized in vitro and incubated with the isolated thylakoid membranes. After such incubation, the subunits were found in the membranes and were resistant to digestion with proteases and removal by 2 molar NaBr. All of the radioactive proteins incorporated in the membrane were found in the photosystem I complex. The subunit II was assembled specifically into cyanobacterial thylakoid membranes and not into Escherichia coli cell membranes or thylakoid membranes isolated from spinach. The assembly process did not require ATP or proton motive force, and it was not stimulated by ATP. The assembly of subunits II and IV into thylakoid membranes isolated from the strain AEK2, which lacks the gene psaE, was increased two- to threefold. The incorporation of subunit II was 15 to 17 times higher in the thylakoids obtained from the strain ADK3 in which the gene psaD has been inactivated. However, assembly of subunit IV in the same thylakoids was reduced by 65%, demonstrating that the presence of subunit II is required for the stable assembly of subunit IV. Large deletions in subunit II prevented its incorporation into thylakoids and assembly into photosystem I, suggesting that the overall conformation of the protein rather than a specific targeting sequence is required for its assembly into photosystem I.
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PMID:Assembly of Two Subunits of the Cyanobacterial Photosystem I on the n-Side of Thylakoid Membranes. 1666 56

KaiA, KaiB, and KaiC are essential proteins of the circadian clock in the cyanobacterium Synechococcus elongatus PCC 7942. The phosphorylation cycle of KaiC that occurs in vitro after mixing the three proteins and ATP is thought to be the master oscillation governing the circadian system. We analyzed the temporal profile of complexes formed between the three Kai proteins. In the phosphorylation phase, KaiA actively and repeatedly associated with KaiC to promote KaiC phosphorylation. High levels of phosphorylation of KaiC induced the association of the KaiC hexamer with KaiB and inactivate KaiA to begin the dephosphorylation phase, which is closely linked to shuffling of the monomeric KaiC subunits among the hexamer. By reducing KaiC phosphorylation, KaiB dissociated from KaiC, reactivating KaiA. We also confirmed that a similar model can be applied in cyanobacterial cells. The molecular model proposed here provides mechanisms for circadian timing systems.
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PMID:Cyanobacterial circadian pacemaker: Kai protein complex dynamics in the KaiC phosphorylation cycle in vitro. 1685 83

Synechococcus elongatus PCC 7942 was able to grow with several S sources. The sulphur metabolizing enzymes viz. ATP sulphurylase, cysteine synthase, thiosulphate reductase and L- and D-cysteine desulphydrases were regulated by sulphur sources, particularly by sulphur amino acids and organic sulphate esters. Sulphur starvation reduced ATP sulphurylase and cysteine synthase whereas reduced glutathione appreciated Cys degradation activity. With partially purified enzymes apparent Km values for sulphate, ATP, D- and L-Cys, thiosulphate, sulphide and O-acetyl serine were in a range of 12-50 microM. p-Nitrophenyl sulphate inhibited ATP sulphurylase competitively. Met was a feedback inhibitor of several key enzymes.
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PMID:Catalytic and regulatory properties of sulphur metabolizing enzymes in cyanobacterium Synechococcus elongatus PCC 7942. 1699 35

Cyanobacteria such as Synechococcus elongatus PCC 7942, Thermosynechococcus elongatus BP-1, and Synechocystis species strain PCC 6803 have an endogenous timing mechanism that can generate and maintain a 24 h (circadian) periodicity to global (whole genome) gene expression patterns. This rhythmicity extends to many other physiological functions, including chromosome compaction. These rhythmic patterns seem to reflect the periodicity of availability of the primary energy source for these photoautotrophic organisms, the Sun. Presumably, eons of environmentally derived rhythmicity--light/dark cycles--have simply been mechanistically incorporated into the regulatory networks of these cyanobacteria. Genetic and biochemical experimentation over the last 15 years has identified many key components of the primary timing mechanism that generates rhythmicity, the input pathways that synchronize endogenous rhythms to exogenous rhythms, and the output pathways that transduce temporal information from the timekeeper to the regulators of gene expression and function. Amazingly, the primary timing mechanism has evidently been extracted from S. elongatus PCC 7942 and can also keep time in vitro. Mixing the circadian clock proteins KaiA, KaiB, and KaiC from S. elongatus PCC 7942 in vitro and adding ATP results in a circadian rhythm in the KaiC protein phosphorylation state. Nonetheless, many questions still loom regarding how this circadian clock mechanism works, how it communicates with the environment and how it regulates temporal patterns of gene expression. Many details regarding structure and function of the individual clock-related proteins are provided here as a basis to discuss these questions. A strong, data-intensive foundation has been developed to support the working model for the cyanobacterial circadian regulatory system. The eventual addition to that model of the metabolic parameters participating in the command and control of this circadian global regulatory system will ultimately allow a fascinating look into whole-cell physiology and metabolism and the consequential organization of global gene expression patterns.
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PMID:A circadian timing mechanism in the cyanobacteria. 1702 73

Three dnaK and four dnaJ genes have been identified in the genome of cyanobacterium Synechococcus elongatus PCC 7942. Our comprehensive analysis of yeast two-hybrid screening revealed a specific interaction among DnaK2, DnaJ2, and RNase E, an essential endoribonuclease. We examined the effects of DnaK2 and DnaJ2 on RNase E activity by monitoring the digestion of psbAII transcript in vitro. The addition of DnaK2 and DnaJ2 obviously inhibited RNase E activity in an ATP-dependent manner. These results suggest that DnaK2 and DnaJ2 are involved in RNA degradation through interaction with RNase E.
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PMID:Protection of psbAII transcript from ribonuclease degradation in vitro by DnaK2 and DnaJ2 chaperones of the cyanobacterium Synechococcus elongatus PCC 7942. 1721 38

Following a N-methyl-N'-nitro-N-nitrosoguanidine-based mutagenesis of Synechococcus elongatus PCC 7942 wild type, we were able to select several mutants with an enhanced tolerance toward the herbicide bentazone (3-isopropyl-1H-2,1,3-benzothiadiazine-4(3H)-one 2,2-dioxide). Mutant Mu1 has in part been previously characterized. In the present paper we report on another mutant, called Mu2, which also has a higher tolerance toward bentazone. Since Mu2 showed a better growth than WT when cultivated with elevated NaCl concentrations in the growth medium and since S. elongatus WT has previously been classified to be low salt tolerant, we were especially interested in the identification of the modifications conferring this higher salt tolerance to mutant Mu2. Immunoblot analyses provided evidence that Mu2 had a constitutively higher expression of PsbO and of IsiA. In addition, in Mu2 a significantly higher concentration of IdiA was detected under salt stress as compared to WT. These three proteins most likely contribute to a better protection and/or stabilization of photosystem II. Moreover, Mu2 had a higher amount of the photosystem I reaction center proteins PsaAB under salt stress than WT. In addition, the amount of the ferredoxin:NADP+ oxidoreductase and also of the ATP synthase was constitutively higher in Mu2 than in WT. In contrast to WT the latter two proteins did not decrease under salt stress in Mu2. Therefore, it can be assumed that Mu2 could maintain a high cyclic electron transport activity around photosystem I under salt stress. It can be assumed that the combination of these modifications of the electron transport chain cause a better protection of photosystem II against oxidative damage and cause an increase of cyclic electron transport activity around photosystem I with ATP synthesis. Thus, the overall cellular energization in Mu2 relative to WT is improved. Together with putative other not yet identified modifications this seems to enable Mu2 to energize its cytoplasmic membrane-localized ion pumps more effectively than WT and, as a consequence, to keep the intracellular NaCl concentration low.
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PMID:A Synechococcus elongatus PCC 7942 mutant with a higher tolerance toward the herbicide bentazone also confers resistance to sodium chloride stress. 1755 35

Enzymes of the ATP-independent Deg serine endopeptidase family are very flexible with regard to their substrate specificity. Some family members cleave only one substrate, while others act as general proteases on unfolded substrates. The proteolytic activity of Deg proteases is regulated by PDZ protein interaction domains. Here we characterized the HhoA protease from Synechocystis sp. strain PCC 6803 in vitro using several recombinant protein constructs. The proteolytic activity of HhoA was found to increase with temperature and basic pH and was stimulated by the addition of Mg(2+) or Ca(2+). We found that the single PDZ domain of HhoA played a critical role in regulating protease activity and in the assembly of a hexameric complex. Deletion of the PDZ domain strongly reduced proteolysis of a sterically challenging resorufin-labeled casein substrate, but unlabeled beta-casein was still degraded. Reconstitution of the purified HhoA with total membrane proteins isolated from Synechocystis sp. wild-type strain PCC 6803 and a DeltahhoA mutant resulted in specific degradation of selected proteins at elevated temperatures. We concluded that a single PDZ domain of HhoA plays a critical role in defining the protease activity and oligomerization state, combining the functions that are attributed to two PDZ domains in the homologous DegP protease from Escherichia coli. Based on this first enzymatic study of a Deg protease from cyanobacteria, we propose a general role for HhoA in the quality control of extracytoplasmic proteins, including membrane proteins, in Synechocystis sp. strain PCC 6803.
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PMID:The serine protease HhoA from Synechocystis sp. strain PCC 6803: substrate specificity and formation of a hexameric complex are regulated by the PDZ domain. 1761 90


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