Expression of Maize Ferredoxin cDNA in Escherichia coli: Comparison of Photosynthetic and Nonphotosynthetic Ferredoxin Isoproteins and their Chimeric Molecule - PubMed (original) (raw)
Expression of Maize Ferredoxin cDNA in Escherichia coli: Comparison of Photosynthetic and Nonphotosynthetic Ferredoxin Isoproteins and their Chimeric Molecule
T Hase et al. Plant Physiol. 1991 Dec.
Abstract
Maize (Zea mays L.) has two types of ferredoxin (Fd) differentially expressed in photosynthetic and nonphotosynthetic organs. A cDNA fragment encoding the mature polypeptide of Fd III, an Fd isoprotein of the nonphotosynthetic type, was expressed in Escherichia coli, and the Fd was synthesized as a holo-form assembled with the [2Fe-2S] cluster, which was completely identical with authentic Fd III prepared from maize roots. This expression system made it possible to prepare Fd present at fairly low levels in plants in amounts sufficient for functional and structural studies. Comparison of electron transfer activity of Fd III with that of Fd I, an Fd isoprotein of the photosynthetic type, showed that Fd III was superior as an electron acceptor from NADPH, and Fd I was superior as an electron donor for NADP(+), in reactions catalyzed by Fd-NADP(+) reductase from maize leaf. The circular dichronism spectra of the two Fds also indicated a subtle difference in the geometry of their iron-sulfur clusters. These results are consistent with the view that photosynthetic and nonphotosynthetic Fds may be functionally differentiated. An artificial chimeric Fd, Fd III/Fd I, whose amino-terminal and carboxylterminal halves are derived from the corresponding regions of Fd III and Fd I, respectively, showed an activity and CD spectrum significantly similar to those of Fd I. This suggests that 18 amino acid substitutions between Fd III and Fd III/Fd I alter the properties of Fd III so that they resemble those of Fd I.
Similar articles
- Plastid import and iron-sulfur cluster assembly of photosynthetic and nonphotosynthetic ferredoxin isoproteins in maize.
Suzuki S, Izumihara K, Hase T. Suzuki S, et al. Plant Physiol. 1991 Sep;97(1):375-80. doi: 10.1104/pp.97.1.375. Plant Physiol. 1991. PMID: 16668395 Free PMC article. - Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins.
Onda Y, Matsumura T, Kimata-Ariga Y, Sakakibara H, Sugiyama T, Hase T. Onda Y, et al. Plant Physiol. 2000 Jul;123(3):1037-45. doi: 10.1104/pp.123.3.1037. Plant Physiol. 2000. PMID: 10889253 Free PMC article. - Analysis of reductant supply systems for ferredoxin-dependent sulfite reductase in photosynthetic and nonphotosynthetic organs of maize.
Yonekura-Sakakibara K, Onda Y, Ashikari T, Tanaka Y, Kusumi T, Hase T. Yonekura-Sakakibara K, et al. Plant Physiol. 2000 Mar;122(3):887-94. doi: 10.1104/pp.122.3.887. Plant Physiol. 2000. PMID: 10712553 Free PMC article. - Evolution of the acceptor side of photosystem I: ferredoxin, flavodoxin, and ferredoxin-NADP+ oxidoreductase.
Pierella Karlusich JJ, Carrillo N. Pierella Karlusich JJ, et al. Photosynth Res. 2017 Dec;134(3):235-250. doi: 10.1007/s11120-017-0338-2. Epub 2017 Feb 1. Photosynth Res. 2017. PMID: 28150152 Review. - The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites.
Seeber F, Aliverti A, Zanetti G. Seeber F, et al. Curr Pharm Des. 2005;11(24):3159-72. doi: 10.2174/1381612054864957. Curr Pharm Des. 2005. PMID: 16178751 Review.
Cited by
- Characterization of a Unique Pair of Ferredoxin and Ferredoxin NADP+ Reductase Isoforms That Operates in Non-Photosynthetic Glandular Trichomes.
Polito JT, Lange I, Barton KE, Srividya N, Lange BM. Polito JT, et al. Plants (Basel). 2024 Jan 30;13(3):409. doi: 10.3390/plants13030409. Plants (Basel). 2024. PMID: 38337942 Free PMC article. - Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin.
Tohda R, Tanaka H, Mutoh R, Zhang X, Lee YH, Konuma T, Ikegami T, Migita CT, Kurisu G. Tohda R, et al. J Biol Chem. 2021 Jan-Jun;296:100217. doi: 10.1074/jbc.RA120.016271. Epub 2020 Dec 24. J Biol Chem. 2021. PMID: 33839679 Free PMC article. - Identification of global ferredoxin interaction networks in Chlamydomonas reinhardtii.
Peden EA, Boehm M, Mulder DW, Davis R, Old WM, King PW, Ghirardi ML, Dubini A. Peden EA, et al. J Biol Chem. 2013 Dec 6;288(49):35192-209. doi: 10.1074/jbc.M113.483727. Epub 2013 Oct 7. J Biol Chem. 2013. PMID: 24100040 Free PMC article. - Pattern of expression and substrate specificity of chloroplast ferredoxins from Chlamydomonas reinhardtii.
Terauchi AM, Lu SF, Zaffagnini M, Tappa S, Hirasawa M, Tripathy JN, Knaff DB, Farmer PJ, Lemaire SD, Hase T, Merchant SS. Terauchi AM, et al. J Biol Chem. 2009 Sep 18;284(38):25867-78. doi: 10.1074/jbc.M109.023622. Epub 2009 Jul 7. J Biol Chem. 2009. PMID: 19586916 Free PMC article. - cDNA cloning, expression levels and gene mapping of photosynthetic and non-photosynthetic ferredoxin genes in sunflower (Helianthus annuus L.).
Venegas-Calerón M, Zambelli A, Ruiz-López N, Youssar L, León A, Garcés R, Martínez-Force E. Venegas-Calerón M, et al. Theor Appl Genet. 2009 Mar;118(5):891-901. doi: 10.1007/s00122-008-0947-4. Epub 2009 Jan 8. Theor Appl Genet. 2009. PMID: 19130032
References
- J Mol Biol. 1990 Nov 20;216(2):399-410 - PubMed
- Science. 1991 Jan 4;251(4989):60-6 - PubMed
- Cell. 1986 Aug 1;46(3):365-75 - PubMed
- Arch Biochem Biophys. 1990 Nov 15;283(1):75-80 - PubMed
- Arch Biochem Biophys. 1987 Aug 1;256(2):430-4 - PubMed
LinkOut - more resources
Full Text Sources