Abstract
A cDNA containing the entire coding region for the iron storage protein ferritin has been isolated from the French bean plant,Phaseolus vulgaris L. cv. Tendergreen. Ferritin protein was purified from young leaves and shoot meristem tissue and used to raise antisera in mice. A λgt11 cDNA library was constructed from seed-derived poly(A)+ RNA, and screened with the mouse anti-ferritin serum. A 1.2 kb immunopositive phage DNA insert was isolated and sequenced. The derived amino acid sequence shows substantial similarity with other ferritin sequences. The 5′ untranslated region contains two out-of-frame AUG codons, a region of extreme pyrimidine composition bias and potentially stable secondary structure.
This is a preview of subscription content, log in via an institution to check access.
References
Aziz N, Munro HN: Both subunits of rat liver ferritin are regulated at a translational level by iron. Nucl Acids Res 14: 915–927 (1986).
Costanzo F, Colombo M, Staempfli S, Santoro C, Marone M, Frank R, Delius H, Cortese R: Structure of gene and pseudogenes of human apoferritin H. Nucl Acids Res 14: 721–736 (1986).
Gubler U, Hoffman BJ: A simple and very efficient method for generating cDNA libraries. Gene 25: 263–269 (1983).
Ishi S, Xu Y, Stratton RH, Roe BA, Merlino GT, Pastan I: Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene. Proc Natl Acad Sci USA 83: 4920–4924 (1985).
Kato M, Kuhoh J, Shimizu N: The pyrimidine/purine-biased region of the epidermal growth factor receptor gene is sensitive to S1 nuclease and may form an intramolecular triplex. Biochem J 268: 175–180 (1990).
Klausner RD, Harford JB: Cis-trans models for post-transcriptional gene regulation. Science 246: 870–872 (1989).
Klickstein LB: Construction of recombinant DNA libraries. In: Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds), Current Protocols in Molecular Biology, pp. 5.5.1.-5.6.8. John Wiley, New York (1987).
Ko MP, Huang P-Y, Huang J-S, Barker KR: The occurrence of phytoferritin and its relationship to effectiveness of soybean nodules. Plant Physiol 83: 299–305 (1987).
Kozak M: The scanning model for translation: an update. J Cell Biol 108: 229–241 (1989).
Lane LC, Skopp RN: A simple method for purifying phytoferritin. J Plant Nutr 9: 661–669 (1986).
Mattia E, den Blaauwen J, Ashwell G, van Renswoude J: Multiple post-transcriptional regulatory mechanisms in ferritin gene expression. Proc Natl Acad Sci USA 86: 1801–1805 (1989).
Pearson WR, Lipman DJ: Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 85: 2444–2448 (1988).
Polites HG, Marotti KR: A step-wise protocol for cDNA synthesis. BioTechniques 4: 514–520 (1986).
Ragland M, Briat J-F, Gagnon J, Laulhere J-P, Massenet O, Theil EC: Evidence for conservation of ferritin sequences amoug plants and animals and for a transit peptide in soybean. J Biol Chem 265: 18339–18344 (1990).
Rouault TA, Hentze M, Caughman SW, Harford JB, Klausner R: Binding of a cytosolic protein to the ironresponsive element of human ferritin messenger RNA. Science 241: 1207–1210 (1988).
Rouault TA, Tang CK, Kaptain S, Burgess WH, Haile DJ, Samaniego F. McBride OW, Harford JB, Klausner R: Cloning of the cDNA encoding an RNA regulatory protein—the human iron-responsive element-binding protein. Proc Natl Acad Sci USA 87: 7958–7962 (1990).
Russel M, Kidd S, Kelly MR: An improved filamentous helper phage for generating single-stranded plasmid DNA. Gene 45: 333–338 (1986).
Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).
Schmidt GW, Mishkind ML: The transport of proteins into chloroplasts. Annu Rev Biochem 55: 879–912 (1986).
Sengupta C, De Luca V, Bailey DS, Verma VPS: Post-translational processing of 7S and 11S components of soybean storage proteins. Plant Mol Biol 1: 19–34 (1981).
Snyder M, Elledge S, Sweetser D, Young RA, Davis RW: λgt11: gene isolation with antibody probes and other applications. In: Wu R, Grossman L (eds), Methods in Enzymology vol 154 pp. 107–128. Academic Press, New York (1987).
Theil EC: Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms. Annu Rev Biochem 56: 289–315 (1987).
Theil EC: Regulation of ferritin and transferrin receptor mRNAs. J Biol Chem 265: 4771–4774 (1990).
van der Mark F, van den Briel W, Huisman HG: Phytoferritin is synthesizedin vitro as a high-molecular-weight precursor. Biochem J 214: 943–950 (1983).
van der Mark F, van den Briel W: Purification and partial characterization of ferritin from normal and ironloaded leaves ofPhaseolus vulgaris. Plant Sci 39: 55–60 (1985).
Walden WE, Patino MM, Gaffield L: Purification of a specific repressor of ferritin mRNA translation from rabbit liver. J Biol Chem 264: 13765–13769 (1989).
Wells RD: Unusual DNA structures. J Biol Chem 263: 1095–1098 (1988).
Zuker M, Stiegler P: Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information. Nucl Acids Res 9: 133–148 (1981).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Spence, M.J., Henzl, M.T. & Lammers, P.J. The structure of aPhaseolus vulgaris cDNA encoding the iron storage protein ferritin. Plant Mol Biol 17, 499–504 (1991). https://doi.org/10.1007/BF00040644
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00040644