Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1832526 (PCC)
 5,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thioredoxin is a small redox protein that functions as a reducing agent and modulator of enzyme activity. A gene for an unusual thioredoxin was previously isolated from the cyanobacterium Anabaena sp. strain PCC 7120 and cloned and expressed in Escherichia coli. However, the protein could not be detected in Anabaena cells (J. Alam, S. Curtis, F. K. Gleason, M. Gerami-Nejad, and J. A. Fuchs, J. Bacteriol. 171:162-171, 1989). Polyclonal antibodies to the atypical thioredoxin were prepared, and the protein was detected by Western immunoblotting. It occurs at very low levels in extracts of Anabaena sp. and other cyanobacteria. No antibody cross-reaction was observed in extracts of eukaryotic algae, plants, or eubacteria. The anti-Anabaena thioredoxin antibodies did react with another unusual thioredoxin-glutaredoxin produced by bacteriophage T4. Like the T4 protein and other glutaredoxins, the unusual cyanobacterial thioredoxin can be reduced by glutathione. The Anabaena protein can also activate enzymes of carbon metabolism and has some functional similarity to spinach chloroplast thioredoxin f. However, it shows only 23% amino acid sequence identity to the spinach chloroplast protein and appears to be distantly related to other thioredoxins. The data indicate that cyanobacteria, like plant chloroplasts, have two dissimilar thioredoxins. One is related to the more common protein found in other prokaryotes, and the other is an unusual thioredoxin that can be reduced by glutathione and may function in glucose catabolism.
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PMID:Activities of two dissimilar thioredoxins from the cyanobacterium Anabaena sp. strain PCC 7120. 155 78

We describe the first complete segregation of a targeted inactivation of psaA encoding one of the P700-chlorophyll a apoproteins of photosystem (PS) I. A kanamycin resistance gene was used to interrupt the psaA gene in the unicellular cyanobacterium Synechocystis sp. PCC 6803. Selection of a fully segregated mutant, ADK9, was performed under light-activated heterotrophic growth (LAHG) conditions; complete darkness except for 5 min of light every 24 h and 5 mM glucose. Under these conditions, wild-type cells showed a 4-fold decrease in chlorophyll (chl) per cell, primarily due to a decrease of PS I reaction centers. Evidence for the absence of PS I in ADK9 includes: the lack of EPR (electron paramagnetic resonance) signal I, from P700+; undetectable P700-apoprotein; greatly reduced whole-chain photosynthesis rates; and greatly reduced chl per cell, resulting in a turquoise blue phenotype. The PS I peripheral proteins PSA-C and PSA-D were not detected in this mutant. ADK9 does assemble near wild-type levels of functional PS II per cell, evidenced by: EPR signal II from YD+; high rates of oxygen evolution with 2,6-dichloro-p-benzoquinone (DCBQ), an electron acceptor from PS II; and accumulation of D1, a PS II core polypeptide. The success of this transformation indicates that this cyanobacterium may be utilized for site-directed mutagenesis of the PS I core.
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PMID:Targeted genetic inactivation of the photosystem I reaction center in the cyanobacterium Synechocystis sp. PCC 6803. 171 64

The variation of endogenous insulin secretion in association with fasting plasma glucose (FPG) level and the modality of treatment was assessed using serum C-peptide levels before and after breakfast and the corrected value of 24-h urinary C-peptide (24 h-UCP) in inpatients with non-insulin-dependent diabetes mellitus. The corrected value calculated as 24 h-UCP/(urinary C-peptide to creatinine clearance (CCP/CCR) ratio in the fasting state x 10) was correlated with the sum of day-long serum C-peptide levels (r = 0.93) more closely than the measured value of 24 h-UCP (r = 0.79) in 9 patients. In 52 patients treated with diet alone, 38 with sulfonylurea and 28 with insulin, fasting serum C-peptide level did not vary with FPG level, and the increment of serum C-peptide level after breakfast and the corrected value of 24 h-UCP decreased with the rise in FPG level in each treatment. These indexes were the lowest in insulin treatment among the patients with similar FPG levels. In conclusion, 24 h-UCP was demonstrated to be able to reflect day-long endogenous insulin secretion more faithfully after the correction with the CCP/CCR ratio. It was estimated that the insulin response to breakfast and day-long insulin secretion decreased with the rise in FPG level, but basal insulin secretion was maintained over a wide range of FPG levels in each treatment. Endogenous insulin secretion seemed to be somewhat suppressed or rested by exogenous insulin in insulin-treated patients.
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PMID:Variation of endogenous insulin secretion in association with treatment status: assessment by serum C-peptide and modified urinary C-peptide. 177 9

The 27-, 30-, and 33-kDa rod linker polypeptides and the 75-kDa core linker of phycobilisomes from the cyanobacterium Synechococcus sp. strain PCC 7942 have been reported to be glycoproteins with carbohydrate contents ranging from 3.2 to 18.8% and composed of N-acetylgalactosamine and glucose (H.C. Riethman, T.P. Mawhinney, and L.A. Sherman, J. Bacteriol. 170:2433-2440, 1988). Synechococcus sp. strain PCC 7942 phycobilisomes were purified extensively, and the linker polypeptides were separated from the phycobiliproteins by precipitation in 1 M NaSCN. Upon hydrolysis, the linker fraction yielded 0.037% glucose and 0.015% galactosamine by weight and no other carbohydrate. Phycobilisome polypeptides separated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate were subjected to various glycoprotein-specific staining procedures. Linker polypeptides showed very weak concanavalin A binding and no staining by the Schiff-periodate method or by a much more sensitive periodate oxidation-based method. These results indicated that the linker polypeptides are not glycosylated. An earlier report (T. Fujiwara, J. Biochem. 49:361-367, 1961) contended, on the basis of the isolation of sugar-containing peptic chromopeptides from Porphyra tenera R-phycoerythrin, that this red algal phycobiliprotein is a glycoprotein. Analysis of Gastroclonium coulteri R-phycoerythrin and Porphyridium cruentum B-phycoerythrin revealed only traces of carbohydrate in these two proteins, 0.36 and 0.14%, respectively. Results of glycoprotein staining of gels suggested that the carbohydrate in the R-phycoerythrin preparation is due to a glycoprotein contaminant and that neither red algal phycoerythrin is glycosylated.
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PMID:Absence of glycosylation on cyanobacterial phycobilisome linker polypeptides and rhodophytan phycoerythrins. 190 14

We have cloned and sequenced the psaA and psaB genes from the unicellular cyanobacterium Synechocystis sp. PCC 6803. These genes are arranged in tandem, are co-transcribed, and are highly homologous to the psaA and psaB genes previously characterized. RNA was isolated from light-grown cells, from cells put in total darkness with and without glucose, and from cells grown under light-activated heterotrophic growth (LAHG) conditions. Quantitation of hybridization to northern blots revealed only a slight decrease in the accumulation of the psaA-psaB transcript in cells grown in complete darkness with glucose and in LAHG cells, relative to light-grown cells. Accumulation of the psbA transcript steadily declines through dark incubation, with a steady-state level in LAHG cells 28% of that in light-grown cells. Transcripts from psbD, psaD, and rbcLS accumulate in cells grown in complete darkness and in LAHG cells to approximately the same levels as in light-grown cells. Photosynthesis gene transcripts in cells grown in the dark without glucose were detected, but were highly degraded. Our data prove that transcripts from photosynthesis genes do accumulate in dark-grown Synechocystis 6803, which may allow for synthesis and assembly of photosystem (PS) I and PS II in the dark.
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PMID:Expression of photosynthesis genes in the cyanobacterium Synechocystis sp. PCC 6803: psaA-psaB and psbA transcripts accumulate in dark-grown cells. 193 86

Synechocystis sp. PCC 6803 is capable of facultative photoheterotrophy with glucose as the sole carbon source. Eight mutants that were unable to take up glucose were transformed with plasmids from pooled gene banks of wild-type Synechocystis DNA prepared in an Escherichia coli vector that does not replicate in Synechocystis. One mutant (EG216) could be complemented with all gene banks to restore ability for photoheterotrophic growth. One of the gene banks was fractionated into single clones and plasmid DNA from each clone used to complement EG216. This yielded a 1.5 kb DNA fragment that was sequenced. It contained one complete open reading frame (gtr) whose putative gene product displayed high sequence conservation with the xylose transporter of E. coli and the mammalian glucose transporters. Further, the isolated gtr gene interrupted in vitro by a kanamycin resistance cassette could be used to construct mutants from wild-type Synechocystis sp. PCC 6803 that lacked a functional glucose transporter, thus confirming the identity of the gtr gene with the glucose transporter gene. This is the first prokaryotic glucose transporter known to share a sequence relationship with mammalian glucose transporters and the first sugar transporter from a cyanobacterium characterized at the sequence level.
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PMID:Sequence conservation among the glucose transporter from the cyanobacterium Synechocystis sp. PCC 6803 and mammalian glucose transporters. 212 97

Fructose was bactericidal for the cyanobacterium Synechocystis sp. strain PCC 6803. Each of ten independently isolated fructose-resistant mutants had an alteration of the glucose transport system, measured as uptake of glucose or of 3-O-methyl-D-glucose. In the presence of the analog, the wild-type Synechocystis strain was protected against fructose. Two mutants altered in photoautotrophy were also isolated.
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PMID:Interaction of fructose with the glucose permease of the cyanobacterium Synechocystis sp. strain PCC 6803. 308 53

Obligate photoheterotrophic mutants of the cyanobacterium Synechocystis sp. PCC 6803 that carry deletions of conserved residues in the plastoquinone-binding niche of the D1 protein were used to select for spontaneous mutations that restore photoautotrophic growth. Spontaneous pseudorevertants emerged from two deletion mutants, delta YNIV246-9 and delta NN266-7, when the cultures were maintained long after the carbon source (glucose) had been depleted from the medium and cells had reached stationary phase. Most pseudorevertants were found to contain tandem duplications of 6-45-base pair DNA sequences located close to the domain carrying the deletion; none of them restored the wild-type sequence. Three pseudorevertants isolated from the delta YNIV246-9 mutant contained a duplication (7-15 codons) of the DNA sequence immediately downstream of the deletion; the protein region encoded by this DNA may include part of the putative de helix, an important constituent of the plastoquinone-binding niche. Three pseudorevertants isolated from the delta NN266-7 mutant contained duplications corresponding to 2-8 amino acid residues adjacent to the site of the deletion. In all six pseudorevertants carrying duplications, the length of the D1 protein in the modified regions was restored to at least the length present in wild type, suggesting that a minimal length of these protein domains may be required for functional integrity. In another photoautotrophic strain isolated from delta NN266-7, no secondary mutations could be identified in the gene coding for the D1 protein; such mutations apparently reside on another protein subunit of the photosystem II complex. Photosystem II function in the pseudorevertants was altered as compared with wild type in terms of growth and oxygen evolution rates, photosystem II concentration, the semiquinone equilibrium at the acceptor side, and thermostability. A mechanism leading to tandem sequence duplication may involve DNA damage followed by DNA synthesis, strand displacement, and ligation.
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PMID:Tandem sequence duplications functionally complement deletions in the D1 protein of photosystem II. 762 58

Photosystem I is a multisubunit pigment-protein complex that functions as a light-driven plastocyanin-ferredoxin oxidoreductase in thylakoid membranes of cyanobacteria and higher plants. A 16-kDa protein subunit of photosystem I complex was isolated from the cyanobacterium Synechocystis sp. PCC 6803. The sequence of its NH2-terminal residues was determined and a corresponding oligonucleotide probe was used to isolate the gene encoding this subunit. The gene, designated as psaL, codes for a protein of 16,605 Da. The deduced amino acid sequence is homologous to the subunit PsaL of barley photosystem I. There are two conserved hydrophobic regions in the subunit PsaL that may cross or interact with thylakoid membranes. The gene psaL exists as a single copy in the genome and is expressed as a monocistronic RNA. Stable mutant strains in which the gene psaL was interrupted by a gene conferring resistance to chloramphenicol, were generated by targeted mutagenesis. Growth and photosynthetic characteristics of a selected mutant strain under photoautotrophic conditions were similar to those of the wild type, suggesting that the function of PsaL is dispensable for photosynthesis in Synechocystis sp. PCC 6803. Western analysis and subunit composition of purified photosystem I revealed that the mutant strain contained other subunits of photosystem I in thylakoid membranes and in the assembled complex. When photosystem II activity was inhibited and glucose was supplied in the medium, mutant strains grew faster than the wild type. Under these conditions of growth, re-reduction of P700 in the mutant cells, but not in the wild type cells, showed a component with an uncharacteristically rapid half-time.
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PMID:Targeted inactivation of the gene psaL encoding a subunit of photosystem I of the cyanobacterium Synechocystis sp. PCC 6803. 768 19

The glnA gene, encoding type I glutamine synthetase (GS) in Synechocystis sp. PCC 6803, showed a high sequence similarity with other cyanobacterial glnA genes. A dramatic decrease in the amount of glnA mRNA, a single transcript of about 1.6 kb, was observed after transfer to darkness, or after incubation with the electron transport inhibitors DCMU or DBMIB. The levels of glnA transcript were fully recovered after 5 min of reillumination. The glnA mRNA was found to be equally stable both in the light and the dark (half-life about 2.5 min). Unlike the glnA messenger, the amount of GS protein was not reduced in the dark. Synthesis of the glnA transcript in the dark required the presence of glucose. In addition, glnA transcription in a Synechocystis psbE-psbF mutant lacking photosystem II required the presence of glucose even when grown in the light. These observations indicate that glnA transcription is under the control of the redox state of the cell. Finally, nitrogen starvation provoked a delay in the decrease of glnA transcript in darkness, suggesting a connection between nitrogen and redox controls of glnA transcript levels.
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PMID:Electron transport controls transcription of the glutamine synthetase gene (glnA) from the cyanobacterium Synechocystis sp. PCC 6803. 772 55


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