Structure, function and regulation of the cyanobacterial high-affinity bicarbonate transporter, BCT1

2002 ◽  
Vol 29 (3) ◽  
pp. 151 ◽  
Author(s):  
Tatsuo Omata ◽  
Yukari Takahashi ◽  
Osamu Yamaguchi ◽  
Takashi Nishimura
Keyword(s):  
Growth Conditions ◽  
Purple Photosynthetic Bacteria ◽  
High Affinity ◽  
Bicarbonate Transporter ◽  
Low Co2 ◽  
Family Protein ◽  
The Family ◽  
Synechococcus Strain ◽  
Synechococcus Sp ◽  
Substrate Binding Protein

The cmpABCD operon of the cyanobacterium Synechococcus sp. strain PCC7942, which is transcribed specifically under CO2-limited growth conditions, encodes an ATP-binding cassette (ABC) transporter involved in HCO3–uptake (designated BCT1). The product of the cmpA gene is a 42-kDa protein anchored to the plasma membrane, which binds HCO3– with high affinity (Kd= 5 µM) and acts as the substrate-binding protein of the transporter. The apparent Km(HCO3–) of BCT1 is 15 µM. BCT1 has the highest affinity for HCO3– among the HCO3– transporters of the Synechococcus strain and is essential for competitive utilization of HCO3– under CO2-limited conditions. BCT1 is closely related to the cyanobacterial nitrate/nitrite transporter (NRT) encoded by the nrtABCD genes. The BCT1 and NRT transporters, together with the putative cyanate transporter of cyanobacteria, comprise a monoanion transporter subfamily in the family of ABC importers. BCT1 and NRT are present in most fresh-water strains of cyanobacteria but seem to be absent in marine cyanobacterial strains. The low CO2-responsive induction of thecmp operon requires a LysR family protein CmpR, which is similar to CbbR (RbcR), the activator of the CO2 fixation operons of chemoautotrophic and purple photosynthetic bacteria.

scholarly journals The Effect of Promoter and RBS Combination on the Growth and Glycogen Productivity of Sodium-Dependent Bicarbonate Transporter (SbtA) Overexpressing Synechococcus sp. PCC 7002 Cells

2021 ◽  
Vol 12 ◽  
Author(s):  
Jai Kumar Gupta ◽  
Shireesh Srivastava
Keyword(s):  
Chlorophyll Content ◽  
Glycogen Content ◽  
Carotenoid Content ◽  
Minor Effect ◽  
Glycogen Accumulation ◽  
High Affinity ◽  
Bicarbonate Transporter ◽  
Sodium Dependent ◽  
Synechococcus Sp ◽  
Carbon Transport

Sodium dependent bicarbonate transporter, SbtA is a high-affinity, inducible bicarbonate transporter in cyanobacterial cells. Our previous work has shown that overexpression of this transporter can significantly increase growth and glycogen accumulation in Synechococcus sp. PCC 7002 cells. In this work, we have tested the effect of two different RBS sequences (RBS1: GGAGGA and RBS2: AGGAGA) and three different promoters (PcpcB, PcpcB560, and PrbcL2) on the growth and glycogen production in SbtA-overexpressing Synechococcus sp. PCC 7002 cells. Our results show that PcpcB or PcpcB560 were more effective than PrbcL2 in increasing the growth and glycogen content. The choice of RBS sequence had relatively minor effect, though RBS2 was more effective than RBS1. The transformant E, with PcpcB560 and RBS2, showed the highest growth. The biomass after 5 days of growth on air or 1% CO2 was increased by about 90% in the strain E compared to PCC 7002 cells. All transformants overexpressing SbtA had higher glycogen content. However, growing the cells with bubbling of 1% CO2 did not increase cellular glycogen content any further. The strain E had about 80% higher glycogen content compared to WT PCC 7002 cells. Therefore, the glycogen productivity of the strain E grown with air-bubbling was about 2.5-fold that of the WT PCC 7002 cells grown similarly. Additionally, some of the transformants had higher chlorophyll content while all the transformants had higher carotenoid content compared to the PCC 7002 cells, suggesting interaction between carbon transport and pigment levels. Thus, this work shows that the choice of photosynthetic promoters and RBSs sequences can impact growth and glycogen accumulation in SbtA-overexpressing cells.

scholarly journals Mechanism of low CO2-induced activation of the cmp bicarbonate transporter operon by a LysR family protein in the cyanobacterium Synechococcus elongatus strain PCC 7942

2008 ◽  
Vol 68 (1) ◽  
pp. 98-109 ◽  
Author(s):  
Takashi Nishimura ◽  
Yukari Takahashi ◽  
Osamu Yamaguchi ◽  
Hiroshi Suzuki ◽  
Shin-ichi Maeda ◽  
...  
Keyword(s):  
Synechococcus Elongatus ◽  
Bicarbonate Transporter ◽  
Low Co2 ◽  
Family Protein ◽  
Pcc 7942 ◽  
Lysr Family

VARIATION IN THE ABUNDANCE OF SYNECHOCOCCUS SP. CC9311 NARB MRNA RELATIVE TO CHANGES IN LIGHT, NITROGEN GROWTH CONDITIONS AND NITRATE ASSIMILATION1

2012 ◽  
Vol 48 (4) ◽  
pp. 1028-1039 ◽  
Author(s):  
Ryan W. Paerl ◽  
Sasha Tozzi ◽  
Zbigniew S. Kolber ◽  
Jonathan P. Zehr
Keyword(s):  
Growth Conditions ◽  
Synechococcus Sp

scholarly journals Involvement of a CbbR Homolog in Low CO2-Induced Activation of the Bicarbonate Transporter Operon in Cyanobacteria

2001 ◽  
Vol 183 (6) ◽  
pp. 1891-1898 ◽  
Author(s):  
Tatsuo Omata ◽  
Satoshi Gohta ◽  
Yukari Takahashi ◽  
Yoshimi Harano ◽  
Shin-ichi Maeda
Keyword(s):  
Specific Binding ◽  
Regulatory Region ◽  
Transcriptional Regulator ◽  
Bisphosphate Carboxylase ◽  
Purple Photosynthetic Bacteria ◽  
Bicarbonate Transporter ◽  
Enhanced Strain ◽  
Operon Expression ◽  
Pcc 7942 ◽  
Pcc 6803

ABSTRACT The cmpABCD operon of Synechococcus sp. strain PCC 7942, encoding a high-affinity bicarbonate transporter, is transcribed only under CO2-limited conditions. InSynechocystis sp. strain PCC 6803, the slr0040, slr0041, slr0043, and slr0044 genes, forming an operon with a putative porin gene (slr0042), were identified as the cmpA, cmpB, cmpC, and cmpDgenes, respectively, on the basis of their strong similarities to the corresponding Synechococcus cmp genes and their induction under low CO2 conditions. Immediately upstream of and transcribed divergently from the Synechocystis cmp operon is a gene (sll0030) encoding a homolog of CbbR, a LysR family transcriptional regulator of the CO2 fixation operons of chemoautotrophic and purple photosynthetic bacteria. Inactivation of sll0030, but not of another closely relatedcbbR homolog (sll1594), abolished low CO2 induction of cmp operon expression. Gel retardation assays showed specific binding of the Sll0030 protein to the sll0030-cmpA intergenic region, suggesting that the protein activates transcription of the cmp operon by interacting with its regulatory region. A cbbR homolog similar to sll0030 and sll1594 was cloned fromSynechococcus sp. strain PCC 7942 and shown to be involved in the low CO2-induced activation of the cmpoperon. We hence designated the Synechocystis sll0030 gene and the Synechococcus cbbR homolog cmpR. In the mutants of the cbbR homologs, upregulation of ribulose-1,5-bisphosphate carboxylase/oxygenase operon expression by CO2 limitation was either unaffected (strain PCC 6803) or enhanced (strain PCC 7942), suggesting existence of other low CO2-responsive transcriptional regulator(s) in cyanobacteria.

Functional characterization of high-affinity Na+/dicarboxylate cotransporter found in Xenopus laevis kidney and heart

2005 ◽  
Vol 289 (5) ◽  
pp. C1159-C1168 ◽  
Author(s):  
Naomi Oshiro ◽  
Ana M. Pajor
Keyword(s):  
Xenopus Laevis ◽  
Cdna Sequence ◽  
Citric Acid Cycle ◽  
Functional Characterization ◽  
Activation Kinetics ◽  
Electrophysiological Properties ◽  
High Affinity ◽  
The Family ◽  
Kidney Liver

The SLC13 gene family includes sodium-coupled transporters for citric acid cycle intermediates and sulfate. The present study describes the sequence and functional characterization of a SLC13 family member from Xenopus laevis, the high-affinity Na+/dicarboxylate cotransporter xNaDC-3. The cDNA sequence of xNaDC-3 codes for a protein of 602 amino acids that is ∼70% identical to the sequences of mammalian NaDC-3 orthologs. The message for xNaDC-3 is found in the kidney, liver, intestine, and heart. The xNaDC-3 has a high affinity for substrate, including a Km for succinate of 4 μM, and it is inhibited by the NaDC-3 test substrates 2,3-dimethylsuccinate and adipate. The transport of succinate by xNaDC-3 is dependent on sodium, with sigmoidal activation kinetics, and lithium can partially substitute for sodium. As with other members of the family, xNaDC-3 is electrogenic and exhibits inward substrate-dependent currents in the presence of sodium. However, other electrophysiological properties of xNaDC-3 are unique and involve large leak currents, possibly mediated by anions, that are activated by binding of sodium or lithium to a single site.

Phosphate-uptake behaviour of a mutant of Synechococcus sp. PCC 7942 lacking one protein of the high-affinity phosphate-uptake system

Planta ◽  
1998 ◽  
Vol 206 (3) ◽  
pp. 461-465 ◽  
Author(s):  
Renate Falkner ◽  
Ferdinand Wagner ◽  
Hirofumi Aiba ◽  
Gernot Falkner
Keyword(s):  
Phosphate Uptake ◽  
Uptake System ◽  
High Affinity ◽  
Synechococcus Sp ◽  
Pcc 7942

scholarly journals Cellular Localization of Carbonic Anhydrase Nce103p in Candida albicans and Candida parapsilosis

2020 ◽  
Vol 21 (3) ◽  
pp. 850
Author(s):  
Jiří Dostál ◽  
Jan Blaha ◽  
Romana Hadravová ◽  
Martin Hubálek ◽  
Olga Heidingsfeld ◽  
...  
Keyword(s):  
Cell Wall ◽  
Candida Albicans ◽  
Carbonic Anhydrase ◽  
Cellular Localization ◽  
Candida Parapsilosis ◽  
Growth Conditions ◽  
Carbonic Anhydrases ◽  
Atmospheric Conditions ◽  
Low Co2 ◽  
Mitochondrial Fractions

Pathogenic yeasts Candida albicans and Candida parapsilosis possess a ß-type carbonic anhydrase Nce103p, which is involved in CO2 hydration and signaling. C. albicans lacking Nce103p cannot survive in low CO2 concentrations, e.g., in atmospheric growth conditions. Candida carbonic anhydrases are orthologous to the Saccharomyces cerevisiae enzyme, which had originally been detected as a substrate of a non-classical export pathway. However, experimental evidence on localization of C. albicans and C. parapsilosis carbonic anhydrases has not been reported to date. Immunogold labeling and electron microscopy used in the present study showed that carbonic anhydrases are localized in the cell wall and plasmatic membrane of both Candida species. This localization was confirmed by Western blot and mass spectrometry analyses of isolated cell wall and plasma membrane fractions. Further analysis of C. albicans and C. parapsilosis subcellular fractions revealed presence of carbonic anhydrases also in the cytosolic and mitochondrial fractions of Candida cells cultivated in shaken liquid cultures, under the atmospheric conditions.

scholarly journals Are sun- and shade-type anatomy required for the acclimation of Neoregelia cruenta?

2013 ◽  
Vol 85 (2) ◽  
pp. 561-574 ◽  
Author(s):  
FERNANDA REINERT ◽  
MARCOS V. LEAL-COSTA ◽  
NICIA E. JUNQUEIRA ◽  
ELIANA S. TAVARES
Keyword(s):  
Growth Conditions ◽  
Sand Ridge ◽  
Light Levels ◽  
The Family ◽  
Sun And Shade ◽  
Shade Leaves ◽  
Sun Leaves ◽  
First Time ◽  
Tank Bromeliads ◽  
Shade Plants

Sun and shade plants are often discriminated by a number of sun- and shade-type anatomies. Nonetheless, we propose that among tank-bromeliads, changes in rosette architecture satisfy the requirements for coping with contrasting light levels. The tank-bromeliad Neoregelia cruenta naturally colonises sub-habitats ranging from full exposure to direct sunlight, to shaded environments in sand ridge plains. We quantified anatomical and morphological traits of leaves and rosettes of N. cruenta grown under sun and shade conditions. Cells with undulated lateral walls within the water parenchyma are for the first time described for the family. Under high light, leaf blades were wider, shorter, and yellowish. The rosette diameter of sun plants was less than half that of shade plants. Sun leaves overlapped with neighbouring leaves for most of their length, forming a cylindrical rosette where water accumulates. Shade leaves only overlapped in the centre of the rosette. Most anatomical traits were similar under both growth conditions. Stomata were absent from the base of sun leaves, which is probably explained by limited gas exchange at the base of the tight sun-type rosette. Data suggest that the ability of N. cruenta to acclimate to sun and shade is better explained by changes in rosette architecture than by leaf anatomy.

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