The Freshwater Cyanobacterium Synechococcus elongatus PCC 7942 Does Not Require an Active External Carbonic Anhydrase
Under standard laboratory conditions, Synechococcus elongatus PCC 7942 lacks EcaASyn, a periplasmic carbonic anhydrase (CA). In this study, a S. elongatus transformant was created that expressed the homologous EcaACya from Cyanothece sp. ATCC 51142. This additional external CA had no discernible eff...
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| Published in: | Plants (Basel) Vol. 13; no. 16; p. 2323 |
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| Main Authors: | , , , |
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| Language: | English |
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| ISSN: | 2223-7747, 2223-7747 |
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| Abstract | Under standard laboratory conditions, Synechococcus elongatus PCC 7942 lacks EcaASyn, a periplasmic carbonic anhydrase (CA). In this study, a S. elongatus transformant was created that expressed the homologous EcaACya from Cyanothece sp. ATCC 51142. This additional external CA had no discernible effect on the adaptive responses and physiology of cells exposed to changes similar to those found in S. elongatus natural habitats, such as fluctuating CO2 and HCO3− concentrations and ratios, oxidative or light stress, and high CO2. The transformant had a disadvantage over wild-type cells under certain conditions (Na+ depletion, a reduction in CO2). S. elongatus cells lacked their own EcaASyn in all experimental conditions. The results suggest the presence in S. elongatus of mechanisms that limit the appearance of EcaASyn in the periplasm. For the first time, we offer data on the expression pattern of CCM-associated genes during S. elongatus adaptation to CO2 replacement with HCO3−, as well as cell transfer to high CO2 levels (up to 100%). An increase in CO2 concentration coincides with the suppression of the NDH-14 system, which was previously thought to function constitutively. |
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| AbstractList | Under standard laboratory conditions, Synechococcus elongatus PCC 7942 lacks EcaASyn, a periplasmic carbonic anhydrase (CA). In this study, a S. elongatus transformant was created that expressed the homologous EcaACya from Cyanothece sp. ATCC 51142. This additional external CA had no discernible effect on the adaptive responses and physiology of cells exposed to changes similar to those found in S. elongatus natural habitats, such as fluctuating CO2 and HCO3− concentrations and ratios, oxidative or light stress, and high CO2. The transformant had a disadvantage over wild-type cells under certain conditions (Na+ depletion, a reduction in CO2). S. elongatus cells lacked their own EcaASyn in all experimental conditions. The results suggest the presence in S. elongatus of mechanisms that limit the appearance of EcaASyn in the periplasm. For the first time, we offer data on the expression pattern of CCM-associated genes during S. elongatus adaptation to CO2 replacement with HCO3−, as well as cell transfer to high CO2 levels (up to 100%). An increase in CO2 concentration coincides with the suppression of the NDH-14 system, which was previously thought to function constitutively. Under standard laboratory conditions, Synechococcus elongatus PCC 7942 lacks EcaASyn, a periplasmic carbonic anhydrase (CA). In this study, a S. elongatus transformant was created that expressed the homologous EcaACya from Cyanothece sp. ATCC 51142. This additional external CA had no discernible effect on the adaptive responses and physiology of cells exposed to changes similar to those found in S. elongatus natural habitats, such as fluctuating CO2 and HCO3- concentrations and ratios, oxidative or light stress, and high CO2. The transformant had a disadvantage over wild-type cells under certain conditions (Na+ depletion, a reduction in CO2). S. elongatus cells lacked their own EcaASyn in all experimental conditions. The results suggest the presence in S. elongatus of mechanisms that limit the appearance of EcaASyn in the periplasm. For the first time, we offer data on the expression pattern of CCM-associated genes during S. elongatus adaptation to CO2 replacement with HCO3-, as well as cell transfer to high CO2 levels (up to 100%). An increase in CO2 concentration coincides with the suppression of the NDH-14 system, which was previously thought to function constitutively.Under standard laboratory conditions, Synechococcus elongatus PCC 7942 lacks EcaASyn, a periplasmic carbonic anhydrase (CA). In this study, a S. elongatus transformant was created that expressed the homologous EcaACya from Cyanothece sp. ATCC 51142. This additional external CA had no discernible effect on the adaptive responses and physiology of cells exposed to changes similar to those found in S. elongatus natural habitats, such as fluctuating CO2 and HCO3- concentrations and ratios, oxidative or light stress, and high CO2. The transformant had a disadvantage over wild-type cells under certain conditions (Na+ depletion, a reduction in CO2). S. elongatus cells lacked their own EcaASyn in all experimental conditions. The results suggest the presence in S. elongatus of mechanisms that limit the appearance of EcaASyn in the periplasm. For the first time, we offer data on the expression pattern of CCM-associated genes during S. elongatus adaptation to CO2 replacement with HCO3-, as well as cell transfer to high CO2 levels (up to 100%). An increase in CO2 concentration coincides with the suppression of the NDH-14 system, which was previously thought to function constitutively. Under standard laboratory conditions, Synechococcus elongatus PCC 7942 lacks EcaASʸⁿ, a periplasmic carbonic anhydrase (CA). In this study, a S. elongatus transformant was created that expressed the homologous EcaACʸᵃ from Cyanothece sp. ATCC 51142. This additional external CA had no discernible effect on the adaptive responses and physiology of cells exposed to changes similar to those found in S. elongatus natural habitats, such as fluctuating CO₂ and HCO₃⁻ concentrations and ratios, oxidative or light stress, and high CO₂. The transformant had a disadvantage over wild-type cells under certain conditions (Na⁺ depletion, a reduction in CO₂). S. elongatus cells lacked their own EcaASʸⁿ in all experimental conditions. The results suggest the presence in S. elongatus of mechanisms that limit the appearance of EcaASʸⁿ in the periplasm. For the first time, we offer data on the expression pattern of CCM-associated genes during S. elongatus adaptation to CO₂ replacement with HCO₃⁻, as well as cell transfer to high CO₂ levels (up to 100%). An increase in CO₂ concentration coincides with the suppression of the NDH-1₄ system, which was previously thought to function constitutively. Under standard laboratory conditions, PCC 7942 lacks EcaA , a periplasmic carbonic anhydrase (CA). In this study, a transformant was created that expressed the homologous EcaA from sp. ATCC 51142. This additional external CA had no discernible effect on the adaptive responses and physiology of cells exposed to changes similar to those found in natural habitats, such as fluctuating CO and HCO concentrations and ratios, oxidative or light stress, and high CO . The transformant had a disadvantage over wild-type cells under certain conditions (Na depletion, a reduction in CO ). cells lacked their own EcaA in all experimental conditions. The results suggest the presence in of mechanisms that limit the appearance of EcaA in the periplasm. For the first time, we offer data on the expression pattern of CCM-associated genes during adaptation to CO replacement with HCO , as well as cell transfer to high CO levels (up to 100%). An increase in CO concentration coincides with the suppression of the NDH-1 system, which was previously thought to function constitutively. |
| Author | Los, Dmitry A. Sinetova, Maria A. Kupriyanova, Elena V. Gabrielyan, David A. |
| AuthorAffiliation | K.A. Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, 127276 Moscow, Russia; sinetova@ifr.moscow (M.A.S.); gabrielyanda@ifr.moscow (D.A.G.); losda@ippras.ru (D.A.L.) |
| AuthorAffiliation_xml | – name: K.A. Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, 127276 Moscow, Russia; sinetova@ifr.moscow (M.A.S.); gabrielyanda@ifr.moscow (D.A.G.); losda@ippras.ru (D.A.L.) |
| Author_xml | – sequence: 1 givenname: Elena V. orcidid: 0000-0002-8266-0461 surname: Kupriyanova fullname: Kupriyanova, Elena V. – sequence: 2 givenname: Maria A. orcidid: 0000-0001-9931-1762 surname: Sinetova fullname: Sinetova, Maria A. – sequence: 3 givenname: David A. orcidid: 0000-0003-4107-1203 surname: Gabrielyan fullname: Gabrielyan, David A. – sequence: 4 givenname: Dmitry A. orcidid: 0000-0002-0142-7853 surname: Los fullname: Los, Dmitry A. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/39204759$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_3389_fphbi_2025_1619812 crossref_primary_10_1038_s41598_025_13711_y crossref_primary_10_3390_plants14142161 |
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| Keywords | CO2-concentrating mechanism NDH-14 cyanobacteria carbonic anhydrase physiological role Cyanothece sp. ATCC 51142 extreme CO2 level Synechococcus elongatus PCC 7942 EcaA |
| Language | English |
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| Snippet | Under standard laboratory conditions, Synechococcus elongatus PCC 7942 lacks EcaASyn, a periplasmic carbonic anhydrase (CA). In this study, a S. elongatus... Under standard laboratory conditions, PCC 7942 lacks EcaA , a periplasmic carbonic anhydrase (CA). In this study, a transformant was created that expressed the... Under standard laboratory conditions, Synechococcus elongatus PCC 7942 lacks EcaASʸⁿ, a periplasmic carbonic anhydrase (CA). In this study, a S. elongatus... |
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| Title | The Freshwater Cyanobacterium Synechococcus elongatus PCC 7942 Does Not Require an Active External Carbonic Anhydrase |
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