Expression of Human Carbonic Anhydrase in the Cyanobacterium Synechococcus PCC7942 Creates a High CO(2)-Requiring Phenotype : Evidence for a Central Role for Carboxysomes in the CO(2) Concentrating Mechanism - PubMed (original) (raw)
Expression of Human Carbonic Anhydrase in the Cyanobacterium Synechococcus PCC7942 Creates a High CO(2)-Requiring Phenotype : Evidence for a Central Role for Carboxysomes in the CO(2) Concentrating Mechanism
G D Price et al. Plant Physiol. 1989 Oct.
Abstract
Active human carbonic anhydrase II (HCAII) protein was expressed in the cyanobacterium Synechococcus PCC7942 by means of transformation with the bidirectional expression vector, pCA. This expression was driven by the bacterial Tac promoter and was regulated by the IacIQ repressor protein, which was expressed from the same plasmid. Expression levels reached values of around 0.3% of total cell protein and this protein appeared to be entirely soluble in nature and located within the cytosol of the cell. The expression of this protein has dramatic effects on the photosynthetic physiology of the cell. Induction of expression of carbonic anhydrase (CA) activity in both high dissolved inorganic carbon (C(i)) and low C(i) grown cells leads the creation of a high C(i) requiring phenotype causing: (a) a dramatic increase in the K(0.5) (C(i)) for photosynthesis, (b) a loss of the ability to accumulate internal C(i), and (c) a decrease in the lag between the initial C(i) accumulation following illumination and the efflux of CO(2) from the cells. In addition, the effects of the expressed CA can largely be reversed by the carbonic anhydrase inhibitor ethoxyzolamide. As a result of the above findings, it is concluded that the CO(2) concentrating mechanism in Synechococcus PCC7942 is largely dependent on (a) the absence of CA activity from the cytosol, and (b) the specific localization of CA activity in the carboxysome. A theoretical model of photosynthesis and C(i) accumulation is developed in which the carboxysome plays a central role as both the site of CO(2) generation from HCO(3(-) ) and a resistance barrier to CO(2) efflux from the cell. There is good qualitative agreement between this model and the measured physiological effects of expressed cytosolic CA in Synechococcus cells.
Similar articles
- Ethoxyzolamide Inhibition of CO(2) Uptake in the Cyanobacterium Synechococcus PCC7942 without Apparent Inhibition of Internal Carbonic Anhydrase Activity.
Price GD, Badger MR. Price GD, et al. Plant Physiol. 1989 Jan;89(1):37-43. doi: 10.1104/pp.89.1.37. Plant Physiol. 1989. PMID: 16666541 Free PMC article. - Association of Carbonic Anhydrase Activity with Carboxysomes Isolated from the Cyanobacterium Synechococcus PCC7942.
Price GD, Coleman JR, Badger MR. Price GD, et al. Plant Physiol. 1992 Oct;100(2):784-93. doi: 10.1104/pp.100.2.784. Plant Physiol. 1992. PMID: 16653059 Free PMC article. - CO2 concentrating mechanisms in cyanobacteria: molecular components, their diversity and evolution.
Badger MR, Price GD. Badger MR, et al. J Exp Bot. 2003 Feb;54(383):609-22. doi: 10.1093/jxb/erg076. J Exp Bot. 2003. PMID: 12554704 Review. - Carboxysomal carbonic anhydrases.
Kimber MS. Kimber MS. Subcell Biochem. 2014;75:89-103. doi: 10.1007/978-94-007-7359-2_6. Subcell Biochem. 2014. PMID: 24146376 Review.
Cited by
- Atomic view of photosynthetic metabolite permeability pathways and confinement in synthetic carboxysome shells.
Sarkar D, Maffeo C, Sutter M, Aksimentiev A, Kerfeld CA, Vermaas JV. Sarkar D, et al. Proc Natl Acad Sci U S A. 2024 Nov 5;121(45):e2402277121. doi: 10.1073/pnas.2402277121. Epub 2024 Nov 1. Proc Natl Acad Sci U S A. 2024. PMID: 39485798 - The Freshwater Cyanobacterium Synechococcus elongatus PCC 7942 Does Not Require an Active External Carbonic Anhydrase.
Kupriyanova EV, Sinetova MA, Gabrielyan DA, Los DA. Kupriyanova EV, et al. Plants (Basel). 2024 Aug 20;13(16):2323. doi: 10.3390/plants13162323. Plants (Basel). 2024. PMID: 39204759 Free PMC article. - A new type of carboxysomal carbonic anhydrase in sulfur chemolithoautotrophs from alkaline environments.
Wieschollek J, Fuller D, Gahramanova A, Millen T, Mislay AJ, Payne RR, Walsh DP, Zhao Y, Carney M, Cross J, Kashem J, Korde R, Lacy C, Lyons N, Mason T, Torres-Betancourt K, Trapnell T, Dennison CL, Chaput D, Scott KM. Wieschollek J, et al. Appl Environ Microbiol. 2024 Sep 18;90(9):e0107524. doi: 10.1128/aem.01075-24. Epub 2024 Aug 23. Appl Environ Microbiol. 2024. PMID: 39177330 - Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP.
Pulsford SB, Outram MA, Förster B, Rhodes T, Williams SJ, Badger MR, Price GD, Jackson CJ, Long BM. Pulsford SB, et al. Sci Adv. 2024 May 10;10(19):eadk7283. doi: 10.1126/sciadv.adk7283. Epub 2024 May 10. Sci Adv. 2024. PMID: 38728392 Free PMC article. - Modeling bacterial microcompartment architectures for enhanced cyanobacterial carbon fixation.
Trettel DS, Pacheco SL, Laskie AK, Gonzalez-Esquer CR. Trettel DS, et al. Front Plant Sci. 2024 Feb 15;15:1346759. doi: 10.3389/fpls.2024.1346759. eCollection 2024. Front Plant Sci. 2024. PMID: 38425792 Free PMC article. Review.
References
- Biochim Biophys Acta. 1965 Nov 29;109(2):448-53 - PubMed
- Gene. 1985;33(1):103-19 - PubMed
- Plant Physiol. 1989 Jan;89(1):37-43 - PubMed
- Plant Physiol. 1989 Jan;89(1):51-60 - PubMed
- Plant Physiol. 1989 Oct;91(2):514-25 - PubMed
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials