Structure of tobacco genes encoding thaumatin-like proteins

Kan, Jan A.L. van; Rhee, M. D. van de; Zuidema, D.; Cornelissen, Ben J. C.; Bol, John F.

doi:10.1007/bf00020500

Cited by 36 publications

(16 citation statements)

References 8 publications

(17 reference statements)

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“…The PR-1a and GRP genes are strongly induced by spraying tobacco with a 5 mM salicylate solution, whereas the PR-S genes are weakly induced by this treatment. A comparison of the putative promoter regions of the PR-la, GRP, and PR-S genes revealed only limited similarities in the first 100 bp upstream of the respective transcription initiation sites (Van Kan et al, 1989). Here we report an analysis of cis-acting elements involved in the induction of the PR-1 a and GRP genes by salicylate treatment and TMV infection.…”

Section: Introductionmentioning

confidence: 86%

“…These clones were used as probes to isolate corresponding genes from a genomic library of Samsun NN tobacco. We reported the complete sequence of the PR-1a gene and two PR-1 pseudogenes , two active PR-S genes (Van Kan et al, 1989), and two genes encoding a glycine-rich protein (GRP) that does not show homology to any of the known PR proteins . In addition, the sequence of the PR-1a gene was reported by severa1 other groups (Ohshima et al, 1987;Payne et al, 1988;Pfitzner et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

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Analysis of regulatory elements involved in the induction of two tobacco genes by salicylate treatment and virus infection.

et al. 1990

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Tobacco genes encoding the PR-la protein and a glycine-rich protein are expressed after treatment of plants with salicylate or infection with tobacco mosaic virus. Upstream sequences of these genes were fused to reporter genes, and these constructs were used to transform tobacco. Upstream sequences of the PR-la gene of 689 base pairs or longer were sufficient for induction of the reporter gene in tobacco mosaic virus-inoculated leaves, systemically induced leaves from infected plants, and leaves treated with salicylate. N o such induction was found with upstream sequences of 643 base pairs or shorter of the PR-la gene. When the PR-la upstream sequence from nucleotides -625 to -902 was fused to the cauliflower mosaic virus 35s core promoter, a construct was obtained that conferred tobacco mosaic virus and salicylate inducibility to the reporter gene in transgenic plants. This confirmed the localization of tobacco mosaic vírus-and salicylate-responsive elements between positions -643 and -689 in the PR-la promoter. With the glycine-rich protein gene, an upstream sequence of 645 base pairs was sufficient for tobacco mosaic virus and salicylate inducibility of the reporter gene, whereas constructs containing 400 base pairs or fewer of the glycine-rich protein promoter were largely inactive.

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Section: Introductionmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Analysis of regulatory elements involved in the induction of two tobacco genes by salicylate treatment and virus infection.

et al. 1990

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“…cDNA probes of the tobacco pathogenesis-related (PR) genes PR-1, PR-2, and PR-5 were synthesized by polymerase chain reaction using synthetic primers to yield fragments of 231 bp (corresponding to positions 507 to 737; Matsuoka et al, 1987), 225 bp (corresponding to positions 1504 to 1728; Linthorst et al, 1990), and 187 bp (corresponding to positions 1781 to 1967; van Kan et al, 1989), respectively. A cDNA probe for the tobacco glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gene was described previously (Seo et al, 1995).…”

Section: Rna Gel Blot Analysismentioning

confidence: 99%

Reduced Levels of Chloroplast FtsH Protein in Tobacco Mosaic Virus–Infected Tobacco Leaves Accelerate the Hypersensitive Reaction

et al. 2000

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In tobacco cultivars resistant to tobacco mosaic virus (TMV), infection results in the death of the infected cells accompanying the formation of necrotic lesions. To identify the genes involved in this hypersensitive reaction, we isolated the cDNA of tobacco DS9, the transcript of which decreases before the appearance of necrotic lesions. The DS9 gene encodes a chloroplastic homolog of bacterial FtsH protein, which serves to maintain quality control of some cytoplasmic and membrane proteins. A large quantity of DS9 protein was found in healthy leaves, whereas the quantity of DS9 protein in infected leaves decreased before the lesions appeared. In transgenic tobacco plants containing less and more DS9 protein than wild-type plants, the necrotic lesions induced by TMV were smaller and larger, respectively, than those on wild-type plants. These results suggest that a decrease in the level of DS9 protein in TMV-infected cells, resulting in a subsequent loss of function of the chloroplasts, accelerates the hypersensitive reaction. INTRODUCTIONThe hypersensitive reaction (HR) is a plant defense system against pathogen attack. HR is defined as the rapid death of infected cells accompanying formation of necrotic lesions in which pathogens are thought to be enclosed (Goodman and Novacky, 1994). The HR of tobacco to tobacco mosaic virus (TMV) occurs in cultivars carrying the resistance gene N ( NN tobacco) but not in cultivars lacking the N gene ( nn tobacco) (Holmes, 1938; Whitham et al., 1994). Induction of the N gene-mediated HR requires the temperature to be below 22 to 26 Њ C (Kassanis, 1952;Shimomura, 1971; Weststeijn, 1981), suggesting that the gene can function at temperatures below this range.We previously observed that when TMV-inoculated leaves were treated with heat shock or actinomycin D, necrotic lesions were induced in not only NN but also in nn tobacco, even at 30 Њ C, a nonpermissive temperature for the N gene (Shimomura and Ohashi, 1971;Ohashi and Shimomura, 1972). In the actinomycin D-treated leaves in which necrotic lesions were induced, the synthesis of nucleic acid in the host plant was greatly suppressed, whereas the synthesis of TMV RNA was suppressed only slightly (Shimomura and Ohashi, 1980). In contrast to treatment with actinomycin D, treatment with other chemicals, including rifampicin, 2-thiouracil, and cycloheximide, which suppress RNA or protein synthesis in both the TMV and the host plant, did not induce necrotic lesions to form (Ohashi and Shimomura, 1972). Given that actinomycin D forms intercalation complexes with DNA, thereby blocking transcription (Waring, 1981), and that heat shock suppresses transcription of housekeeping genes (Lindquist, 1986;Nover et al., 1989), we hypothesized that suppressing the transcription of certain housekeeping genes in NN tobacco plants after infection with TMV could induce the HR.To isolate such candidate genes, we used a synchronous HR-inducing system based on a temperature shift. Incubation at 30 Њ C of TMV-infected NN tobacco leaves results in 1 Curr...

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“…The N-terminus of the polypeptide was confirmed by sequencing the first 39 amino acids ofthe intact protein. Figure 3 shows a sequence comparison of soybean P21 with structurally similar polypeptides from tobacco (1,12), maize (9), and the fruits ofthe monocot Thaumatococcus danieilhi Benth, a West African shrub (14). The amino acid identity shared between these previously characterized proteins and P21 ranges from a high of 71% for tobacco PR-R to a low of 64% with thaumatin.…”

Section: Resultsmentioning

confidence: 99%

Complete Amino Acid Sequence of Soybean Leaf P21

Graham¹,

Burkhart²,

Xiong³

et al. 1992

Plant Physiol.

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A polypeptide structurally related to the thaumatin family of proteins has been purified from soybean (Glycine max) leaves and the complete amino acid sequence has been determined.The mature protein, which we have termed P21, has a calculated molecular weight of 21,461 and an isoelectric point of 4.6. The soybean protein shows 64% amino acid identity with thaumatin, a sweet-tasting protein found in the West African shrub Thaumatococcus danieII, and as much as 71% identity with thaumatinlike polypeptides present in tobacco and maize.were applied to a phenyl-Sepharose column (1.0 x 10.0 cm; Sigma Chemical Co.) equilibrated with 25 mM Na2HPO4, 1 M (NH4)2SO4, pH 7.5. Bound material was eluted with a decreasing linear gradient of (NH4)2SO4 in 25 mM Na2HPO4, pH 7.5. Protein exhibiting proteolytic activity eluting at approximately 250 mM (NH4)2SO4 was collected (data not shown), dialyzed against 25 mm Na2HPO4 (pH 7.5), and subjected to reverse-phase HPLC using a polypore phenyl column (2.1 x 100 mm, Brownlee). Protein was eluted at 50°C with a linear gradient ofacetonitrile (20-90% in 30 min) in 0.1% TFA. The major protein peak was collected for chemical sequencing.Recent reports have shown that certain plants express a group ofpolypeptides that show extensive amino acid identity with the sweet-tasting protein, thaumatin. These thaumatinlike polypeptides include PR-R,3 a tobacco mosaic virus and salicylic acid-inducible polypeptide in tobacco (1, 7, 8); osmotin, an ABA/salt stress-inducible polypeptide (10, 12); and the maize trypsin/a-amylase inhibitor (9). Although the function of the maize bifunctional inhibitor as an anti-nutritive agent is clear, the physiological function of the tobacco polypeptides remains to be elucidated.In this communication, we report the entire amino acid sequence of a polypeptide purified from mature leaves of soybean (Glycine max) that we have termed P21.4 Examination of the amino acid sequence of P21 reveals a striking similarity to the thaumatin-like family of proteins and clearly establishes a homologous counterpart in the legumes. MATERIALS AND METHODS Protein PurificationLeaves of 60-d-old plants (Glycine max var Williams 82) grown in greenhouse conditions were used for the purification. The isolation of the PR-R-like polypeptide was accomplished as previously described for the isolation of a soybean leaf metalloendoproteinase up through P-60 chromatography (4). Following this step, fractions containing proteolytic activity 'Supported by Ohio Board of Regents.

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Structure of tobacco genes encoding thaumatin-like proteins

Cited by 36 publications

References 8 publications

Analysis of regulatory elements involved in the induction of two tobacco genes by salicylate treatment and virus infection.

Analysis of regulatory elements involved in the induction of two tobacco genes by salicylate treatment and virus infection.

Reduced Levels of Chloroplast FtsH Protein in Tobacco Mosaic Virus–Infected Tobacco Leaves Accelerate the Hypersensitive Reaction

Complete Amino Acid Sequence of Soybean Leaf P21

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