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Plant Physiol. Jan 1995; 107(1): 13–23.
PMCID: PMC161159

Accumulation of 15-Kilodalton Zein in Novel Protein Bodies in Transgenic Tobacco.

Abstract

Zeins, the seed storage proteins of maize, are a group of alcohol-soluble polypeptides of different molecular masses that share a similar amino acid composition but vary in their sulfur amino acid composition. They are synthesized on the rough endoplasmic reticulum (ER) in the endosperm and are stored in ER-derived protein bodies. Our goal is to balance the amino acid composition of the methionine-deficient forage legumes by expressing the sulfur amino acid-rich 15-kD zeins in their leaves. However, it is crucial to know whether this protein would be stable in nonseed tissues of transgenic plants. The major focus of this paper is to compare the accumulation pattern of the 15-kD zein protein with a vacuolar targeted seed protein, [beta]-phaseolin, in nonseed tissues and to determine the basis for its stability/instability. We have introduced the 15-kD zein and bean [beta]-phaseolin-coding sequences behind the 35S cauliflower mosaic virus promoter into tobacco (Nicotiana tabacum) and analyzed the protein's accumulation pattern in different tissues. Our results demonstrate that the 15-kD seed protein is stable not only in seeds but in all nonseed tissues tested, whereas the [beta]-phaseolin protein accumulated only in mid- and postmaturation seeds. Interestingly, zein accumulates in novel protein bodies both in the seeds and in nonseed tissues. We attribute the instability of the [beta]-phaseolin protein in nonseed tissues to the fact that it is targeted to protease-rich vacuoles. The stability of the 15-kD zein could be attributed to its retention in the ER or to the protease-resistant nature of the protein.

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Selected References

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  • Bagga S, Sutton D, Kemp JD, Sengupta-Gopalan C. Constitutive expression of the beta-phaseolin gene in different tissues of transgenic alfalfa does not ensure phaseolin accumulation in non-seed tissue. Plant Mol Biol. 1992 Sep;19(6):951–958. [PubMed]
  • Boller T, Kende H. Hydrolytic enzymes in the central vacuole of plant cells. Plant Physiol. 1979 Jun;63(6):1123–1132. [PMC free article] [PubMed]
  • Edwards GA, Hepher A, Clerk SP, Boulter D. Pea lectin is correctly processed, stable and active in leaves of transgenic potato plants. Plant Mol Biol. 1991 Jul;17(1):89–100. [PubMed]
  • Fontes EB, Shank BB, Wrobel RL, Moose SP, OBrian GR, Wurtzel ET, Boston RS. Characterization of an immunoglobulin binding protein homolog in the maize floury-2 endosperm mutant. Plant Cell. 1991 May;3(5):483–496. [PMC free article] [PubMed]
  • Gallie DR, Sleat DE, Watts JW, Turner PC, Wilson TM. A comparison of eukaryotic viral 5'-leader sequences as enhancers of mRNA expression in vivo. Nucleic Acids Res. 1987 Nov 11;15(21):8693–8711. [PMC free article] [PubMed]
  • Hoffman LM, Donaldson DD, Bookland R, Rashka K, Herman EM. Synthesis and protein body deposition of maize 15-kd zein in transgenic tobacco seeds. EMBO J. 1987 Nov;6(11):3213–3221. [PMC free article] [PubMed]
  • A simple and general method for transferring genes into plants. Science. 1985 Mar 8;227(4691):1229–1231. [PubMed]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed]
  • Larkins BA, Hurkman WJ. Synthesis and deposition of zein in protein bodies of maize endosperm. Plant Physiol. 1978 Aug;62(2):256–263. [PMC free article] [PubMed]
  • Lending CR, Larkins BA. Changes in the zein composition of protein bodies during maize endosperm development. Plant Cell. 1989 Oct;1(10):1011–1023. [PMC free article] [PubMed]
  • Li X, Wu Y, Zhang DZ, Gillikin JW, Boston RS, Franceschi VR, Okita TW. Rice prolamine protein body biogenesis: a BiP-mediated process. Science. 1993 Nov 12;262(5136):1054–1056. [PubMed]
  • Ohtani T, Galili G, Wallace JC, Thompson GA, Larkins BA. Normal and lysine-containing zeins are unstable in transgenic tobacco seeds. Plant Mol Biol. 1991 Jan;16(1):117–128. [PubMed]
  • Pedersen K, Argos P, Naravana SV, Larkins BA. Sequence analysis and characterization of a maize gene encoding a high-sulfur zein protein of Mr 15,000. J Biol Chem. 1986 May 15;261(14):6279–6284. [PubMed]
  • Pelham HR. The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem Sci. 1990 Dec;15(12):483–486. [PubMed]
  • Schernthaner JP, Matzke MA, Matzke AJ. Endosperm-specific activity of a zein gene promoter in transgenic tobacco plants. EMBO J. 1988 May;7(5):1249–1255. [PMC free article] [PubMed]
  • van der Valk HC, van Loon LC. Subcellular Localization of Proteases in Developing Leaves of Oats (Avena sativa L.). Plant Physiol. 1988 Jun;87(2):536–541. [PMC free article] [PubMed]
  • Wandelt CI, Khan MR, Craig S, Schroeder HE, Spencer D, Higgins TJ. Vicilin with carboxy-terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants. Plant J. 1992 Mar;2(2):181–192. [PubMed]
  • Wilkins TA, Bednarek SY, Raikhel NV. Role of propeptide glycan in post-translational processing and transport of barley lectin to vacuoles in transgenic tobacco. Plant Cell. 1990 Apr;2(4):301–313. [PMC free article] [PubMed]

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