Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0031511 (pheochromocytoma)
 14,622 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In order to investigate the role and function of the hydrophilic region between transmembrane regions V and CI in the photosystem II core antenna protein CP43, we introduced eight different deletions in psbC of Synechocystis sp; PCC 6803 resulting in a loss of 7-11 codons in evolutionary conserved domains in this region. All deletions resulted in an obligate photoheterotrophic phenotype (requirement of glucose for cell growth) and the absence of any detectable oxygen evolution activity. The various deletion mutations showed a different impact on the amount of CP43 in the thylakoid, ranging from wild-type levels of (a now slightly smaller) CP43 to no detectable CP43 at all. All deletions led to a decrease in the amount of the D1 and D2 proteins in the thylakoids with a larger effect on D2 than on D1. CP47, the other major chlorophyll-binding protein, was present in reduced but significant amounts in the thylakoid. Herbicide binding (diuron) was lost in all but one mutant indicating the PSII components are not assembled into functionally intact complexes. Fluorescence-emission spectra confirmed this notion. This indicates that the large hydrophilic loop of CP43 plays an important role in photosystem II, and even though a shortened CP43 is present in thylakoids of most mutants, functional characteristics resembled that of a mutant with interrupted psbC.
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PMID:Deletion mutations in a long hydrophilic loop in the photosystem II chlorophyll-binding protein CP43 in the cyanobacterium Synechocystis sp. PCC 6803. 821 45

Site-directed mutagenesis has been used to change conserved histidine residues in hydrophobic regions of the photosystem II chlorophyll-binding protein CP47 in the cyanobacterium Synechocystis sp. PCC 6803. Nine mutants with one, four mutants with two, and four mutants with three His mutations in CP47 have been generated and characterized. Mutation of any one of seven different His residues to Tyr leads to slower photoautotrophic growth and apparent destabilization of the PS II complex. Mutations introduced into multiple His residues in one mutant exhibited a cumulative effect. Replacing His by Asn leads to a much smaller effect than observed upon mutation to Tyr. This is consistent with the hypothesis that the mutated His residues are chlorophyll ligands: Asn can substitute as chlorophyll ligand, whereas Tyr cannot. Further evidence supporting a role of the mutated His residues in chlorophyll binding comes from measurements of the light intensity needed to half-saturate oxygen evolution. All His mutants with impaired PS II function needed higher light intensities for half-saturation than wild type. A possible explanation for this decrease in antenna efficiency in the mutants is a loss of the Mg in the chlorophyll due to a loss of the fifth ligand, and thus the formation of a pheophytin molecule in the antenna. We conclude that conserved His residues in hydrophobic regions of CP47 indeed are chlorophyll ligands and that these ligands are important for PS II stability as well as efficient antenna function.
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PMID:Mutation of histidine residues in CP47 leads to destabilization of the photosystem II complex and to impairment of light energy transfer. 849 86

Photosystem I preparations were obtained from wild-type tobacco Nicotiana tabacum var. JWB, three chlorophyll-deficient tobacco mutants: Su/su, Su/su var. Aurea and yellow-green leaf patches of the variegated mutant NC 95, Spinacia oleracea and furthermore from the mesophilic cyanobacterium Synechococcus PCC 7942 and the thermophilic cyanobacterium Synechococcus sp.. Peptides from these preparations were analyzed by SDS polyacrylamide gel electrophoresis and transferred for detection of bound lipids and carotenoids according to the Western blot procedure to nitrocellulose membranes. The PS I preparations from the Nicotiana tabacum species and spinach consist of the core complex and the LHCP I complex, the latter containing, however, traces of the LHCP II polypeptides. The core complex consists of the two core peptides with the apparent molecular mass of 66 kDa each and peptides with molecular masses of 22, 20, 19, 17, 16, 10 and 9 kDa. The LHCP I complex contains 4 subunits with molecular masses of 28, 26, 25 and 24 kDa. The PS I preparations of the two mutants Su/su and Su/su var. Aurea contain as impurities traces of the core peptides (D1/D2) and the two chlorophyll-binding peptides (CP43/CP47) of photosystem II. The PS I preparation from the mesophilic and thermophilic cyanobacterium consists of the two core peptides with the apparent molecular mass of 66 kDa and peptides with molecular masses of 16, 14 and 10 kDa. The peptides of the PS I preparations were characterized by specific PS I, CP I and LHCP I antisera. The antiserum to the PS I complex reacts in the Western blot with the homologous peptides of PS I from higher plants, but only with the CP I complex from the two cyanobacteria. In comparative studies with PS II from higher plants the PS I antiserum reacts with the LHCP II complex as expected. The antiserum to the CP I complex reacts only with the 66 kDa peptides of PS I from all objects. There is no cross reaction with the 66 kDa peptides (heterodimer of the D1/D2 peptides) of PS II. The antiserum to the LHCP I complex reacts only with the four LHCP I peptides of PS I from higher plants and as expected with the LHCP II of PS II: Because cyanobacteria do not have LHCP complexes, there is no reaction with the LHCP I antiserum. By means of polyclonal monospecific antisera to lipids it was shown by Western blot procedure that only two lipid species are bound to PS I peptides. The galactolipid monogalactosyldiglyceride is bound to the CP I complex of the Nicotiana tabacum species, spinach and the two cyanobacteria as well as to the LHCP I complex of the higher plants. The phospholipid phosphatidylglycerol is only associated with the CP I complex of the analyzed higher plants and cyanobacteria. With polyclonal monospecific antisera to carotenoids it was demonstrated that beta-carotene, lutein, neoxanthin and zeaxanthin are associated with the CP I complex of the higher plants and the cyanobacteria analyzed. Violaxanthin is also bound to the CP I complex of the two cyanobacteria, whereas it is bound together with neoxanthin to the LHCP I complex of the higher plants.
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PMID:Comparative immunological detection of lipids and carotenoids on peptides of photosystem I from higher plants and cyanobacteria. 866 97

The requirement of cytochrome c-550 (PSII-V) in photosystem II (PSII) has been assessed in Synechocystis sp. PCC 6803 containing mutations between Gly-351 and Thr-436 of the loop E domain of the chlorophyll a-binding protein CP47. Six photoautotrophic strains were utilized to compare the effect of removal of either the manganese-stabilizing protein (PSII-O) or PSII-V on PSII activity in vivo. These were a wild-type control; two strains with amino acid deletions, Delta(R384-V392) and Delta(G429-T436); and three carrying specific amino acid substitutions, G351L/T365Q, G351L/E364Q/T365Q, and G351L/E353Q/E355Q/T365Q. The removal of PSII-O prevented the assembly of PSII in Delta(G429-T436) but not in Delta(R384-V392). Neither Delta(G429-T436) nor Delta(R384-V392) could support photoautotrophic growth in the absence of PSII-V. In chloride-limiting conditions, the photoautotrophic growth of Delta(R384-V392) was severely impaired and that of Delta(G429-T436) totally inhibited, and no strains lacking PSII-V could grow in chloride-limiting or calcium-limiting media. Substitutions at Gly-351, Glu-353, Glu-355, and Thr-365 produced phenotypes that were similar to those of the control in the presence or absence of PSII-O and PSII-V, but removal of PSII-O from G351L/E364Q/T365Q produced a significant reduction of assembled PSII centers and an enhanced sensitivity to photoinactivation while removal of PSII-V prevented photoautotrophic growth. The additional mutants E364Q:DeltaPSII-V and E364G:DeltaPSII-V demonstrated that this inhibition was a consequence of the mutation at Glu-364. These results also show that the removal of PSII-V, in vivo, produces phenotypes in the CP47 mutants examined that are either similar or more severe than those resulting from the removal of PSII-O.
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PMID:Specific requirements for cytochrome c-550 and the manganese-stabilizing protein in photoautotrophic strains of Synechocystis sp. PCC 6803 with mutations in the domain Gly-351 to Thr-436 of the chlorophyll-binding protein CP47. 977 70

The deletion of the amino acids between Gly-351 and Thr-365 within the large, lumen-exposed, hydrophilic region (loop E) of the photosystem II (PSII) chlorophyll a-binding protein CP47 produced a strain of Synechocystis sp. PCC 6803 that failed to assemble stable PSII centers [Eaton-Rye, J. J., and Vermaas, W. F. J. (1991) Plant Mol. Biol. 17, 1165-1177]. The importance of two conserved Phe residues at positions 362 and 363 within this deletion has been investigated. The F363R strain had impaired photoautotrophic growth and an enhanced sensitivity to photoinactivation, demonstrating that Phe is required at position 363 for normal PSII function. In contrast, photoautotrophic growth in strains N361K and F362R was unaffected. Uniquely, among the mutant strains tested, F363R was unable to grow under chloride-limiting conditions, and this effect was reversed by replacing chloride with bromide. The removal of the manganese-stabilizing protein (PSII-O), the 12 kDa extrinsic protein (PSII-U), and cytochrome c-550 (PSII-V) was investigated in each mutant in vivo. In N361K and F362R, removal of PSII-V produced a more deleterious effect than the removal of PSII-O, but even so, all strains remained photoautotrophic. In contrast, the absence of PSII-V and PSII-O in F363R produced obligate photoheterotrophic strains. The removal of PSII-U increased the susceptibility of PSII to heat inactivation and further decreased the stability of PSII in F363R, demonstrating that PSII-U can contribute to the stabilization of mutations that have been introduced into CP47. The order of importance of the selective removal of the extrinsic proteins in strains carrying mutations in loop E of CP47 was found to be as follows: DeltaPSII-V >/= DeltaPSII-O > DeltaPSII-U.
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PMID:Mutation of Phe-363 in the photosystem II protein CP47 impairs photoautotrophic growth, alters the chloride requirement, and prevents photosynthesis in the absence of either PSII-O or PSII-V in Synechocystis sp. PCC 6803. 1005 41

An Arabidopsis thaliana chlorophyll(ide) a oxygenase gene (cao), which is responsible for chlorophyll b synthesis from chlorophyll a, was introduced and expressed in a photosystem I-less strain of the cyanobacterium Synechocystis sp. PCC 6803. In this strain, most chlorophyll is associated with the photosystem II complex. In line with observations by Satoh et al. [Satoh, S., Ikeuchi, M., Mimuro, M. & Tanaka, A. (2001) J. Biol. Chem. 276, 4293-4297], chlorophyll b was made but accounted for less than 10% of total chlorophyll. However, when lhcb encoding light-harvesting complex (LHC)II from pea was present in the same strain (lhcb(+)/cao(+)), chlorophyll b accumulated in the cell to levels exceeding those of chlorophyll a, although LHCII did not accumulate. In the lhcb(+)/cao(+) strain, the total amount of chlorophyll, the number of chlorophylls per photosystem II center, and the oxygen-evolving activity on a per-chlorophyll basis were similar to those in the photosystem I-less strain. Furthermore, the chlorophyll a/b ratio of photosystem II core particles (retaining CP47 and CP43) and of whole cells of the lhcb(+)/cao(+) strain was essentially identical, and PS II activity could be obtained efficiently by chlorophyll b excitation. These data indicate that chlorophyll b functionally substitutes for chlorophyll a in photosystem II. Therefore, the availability of chlorophylls, rather than their binding specificity, may determine which chlorophyll is incorporated at many positions of photosystem II. We propose that the transient presence of a LHCII/chlorophyll(ide) a oxygenase complex in the lhcb(+)/cao(+) strain leads to a high abundance of available chlorophyll b that is subsequently incorporated into photosystem II complexes. The apparent LHCII requirement for high chlorophyll(ide) a oxygenase activity may be instrumental to limit the occurrence of chlorophyll b in plants to LHC proteins.
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PMID:Chlorophyll b can serve as the major pigment in functional photosystem II complexes of cyanobacteria. 1171 69

The PsbH protein, a small subunit of the photosystem II complex (PSII), was identified as a 6-kDa protein band in the PSII core and subcore (CP47-D1-D2-cyt b-559) from the wild-type strain of the cyanobacterium Synechocystis PCC 6803. The protein was missing in the D1-D2-cytochrome b-559 complex and also in all PSII complexes isolated from IC7, a mutant lacking the psbH gene. The following properties of PSII in the mutant contrasted with those in wild-type: (a) CP47 was released during nondenaturing electrophoresis of the PSII core isolated from IC7; (b) depletion of CO2 resulted in a reversible decrease of the QA- reoxidation rate in the IC7 cells; (c) light-induced decrease in PSII activity, measured as 2,5-dimethyl-benzoquinone-supported Hill reaction, was strongly dependent on the HCO3- concentration in the IC7 cells; and (d) illumination of the IC7 cells lead to an extensive oxidation, fragmentation and cross-linking of the D1 protein. We did not find any evidence for phosphorylation of the PsbH protein in the wild-type strain. The results showed that in the PSII complex of Synechocystis attachment of CP47 to the D1-D2 heterodimer appears weakened and binding of bicarbonate on the PSII acceptor side is destabilized in the absence of the PsbH protein.
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PMID:Absence of the psbH gene product destabilizes photosystem II complex and bicarbonate binding on its acceptor side in Synechocystis PCC 6803. 1185 20

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.
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PMID:Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides. 1206 91

After interruption or deletion of the photosystem II genes psbB, psbC, and psbD in the cyanobacterium Synechocystis sp. PCC 6803, thylakoids from such mutants were found to be depleted in a number of photosystem II proteins in addition to those for which the gene(s) had been inactivated. Transcript levels of photosystem II genes were measured and protein pulse-labeling was carried out to determine the reason for this effect. Transcripts of all photosystem II genes except the inactivated one(s) were found to be present in the various mutants. In certain cases, inactivation of one photosystem II gene led to overexpression of another. Protein pulse-labeling experiments using 35S-methionine, in which not only the rapidly turning over D1 protein but also D2, CP43, and CP47 appear to be preferentially labeled, showed that the mutants studied synthesize the D1 protein as well as other photosystem II proteins whose genes were not inactivated. The fact that, in the various mutants, photosystem II proteins for which the gene is not inactivated are synthesized but do not accumulate in the thylakoid indicates that the psbB, psbC, and psbD gene products are all required for a stable assembly of the photosystem II complex.
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PMID:Transcript Levels and Synthesis of Photosystem II Components in Cyanobacterial Mutants with Inactivated Photosystem II Genes. 1235 60

This chapter contains the description of several methods used for the isolation of functional photosystem (PS)II core particles from wild-type (wt), PSI-less, and CP47 histidine-tagged cells of the cyanobacterium Synechocystis sp. PCC 6803. These protocols discuss the cultivation of PSI-containing and PSI-less cells, isolation of thylakoid membranes, purification of PSII core particles using a weak cation exchange or metal affinity column chromatography, and characterization of the final preparation. The described isolation procedures, which normally yield PSII particles highly active in oxygen evolution, can be easily adapted for obtaining preparations from different types of Synechocystis mutants with modified PSII.
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PMID:Isolation of functional photosystem II core particles from the Cyanobacterium synechocystis sp. PCC 6803. 1518 66


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