Leaf disc transformation of cultivated tomato (L. esculentum) using Agrobacterium tumefaciens

McCormick, Sheila; Niedermeyer, Jeanne G.; Fry, Joyce; Barnason, Arlene; Horsch, Robert B.; Fraley, Robert T.

doi:10.1007/bf00269239

Cited by 507 publications

(254 citation statements)

References 14 publications

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“…Polymerized YK20, YK8, and YL8 inserts were then ligated between SS tob and EGFP as described above for FK9 to form plasmids pUC18-SS tob (32). Tobacco BY-2 cell cultures were transformed by A. tumefaciens infection as detailed previously (33). Transformed tobacco cells were selected on solid media, either Murashige-Skoog medium, Schenk and Hildebrandt (SH), or modified SH lacking kinetin but supplemented with kanamycin (200 g ml Ϫ1 ) and timentin (400 g ml Ϫ1 ) for 2-4 generations as described earlier (25,26).…”

Section: Methodsmentioning

confidence: 99%

Di-isodityrosine Is the Intermolecular Cross-link of Isodityrosine-rich Extensin Analogs Cross-linked in Vitro

Held

Li²,

Kamyab³

et al. 2004

Journal of Biological Chemistry

107

129

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Extensins are cell wall hydroxyproline-rich glycoproteins that form covalent networks putatively involving tyrosyl and lysyl residues in cross-links catalyzed by one or more extensin peroxidases. The precise cross-links remain to be chemically identified both as network components in muro and as enzymic products generated in vitro with native extensin monomers as substrates. However, some extensin monomers contain variations within their putative cross-linking motifs that complicate cross-link identification. Other simpler extensins are recalcitrant to isolation including the ubiquitous P3-type extensin whose major repetitive motif, Ser-(Hyp) 4 -Ser-Hyp-Ser-(Hyp) 4 -Tyr-Tyr-Tyr-Lys, is of particular interest, not least because its Tyr-Tyr-Tyr intramolecular isodityrosine cross-link motifs are also putative candidates for further intermolecular cross-linking to form di-isodityrosine. Therefore, we designed a set of extensin analogs encoding tandem repeats of the P3 motif, including Tyr 3 Phe and Lys 3 Leu variations. Expression of these P3 analogs in Nicotiana tabacum cells yielded glycoproteins with virtually all Pro residues hydroxylated and subsequently arabinosylated and with likely galactosylated Ser residues. This was consistent with earlier analyses of P3 glycopeptides isolated from cell wall digests and the predictions of the Hyp contiguity hypothesis. The tyrosine-rich P3 analogs also contained isodityrosine, formed in vivo. Significantly, these isodityrosine-containing analogs were further crosslinked in vitro by an extensin peroxidase to form the tetra-tyrosine intermolecular cross-link amino acid diisodityrosine. This is the first identification of an intermolecular cross-link amino acid in an extensin module and corroborates earlier suggestions that di-isodityrosine represents one mechanism for cross-linking extensins in muro.Hydroxyproline-rich glycoproteins (HRGPs), 1 which include the extensins, proline-rich proteins, and arabinogalactan proteins (AGPs), contribute to extracellular matrix architecture throughout the plant kingdom and the chlorophycean green algae (1-3). HRGPs are involved in all aspects of plant growth and development, including wall assembly during embryogenesis (4), and responses to biotic and abiotic stress that include mechanical stress (5), physical wounding (6), pathogenesis (7), and symbiosis (8 -10).HRGPs are extended macromolecules consisting of small repetitive peptide and glycopeptide motifs that form peptide modules and glycomodules of functional significance, as in "mix-and-match" mode they define the molecular properties of the overall macromolecule. The glycomodules result from a combination of post-translational modifications unique to plants, namely proline hydroxylation (11) and its subsequent glycosylation (12) that leads either to short arabino-oligosaccharide or larger arabinogalactan polysaccharide addition to the Hyp residues. A sequence-dependent O-Hyp glycosylation code directs the addition of oligosaccharide and polysaccharides (13), and it is likely that...

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Section: Methodsmentioning

confidence: 99%

Di-isodityrosine Is the Intermolecular Cross-link of Isodityrosine-rich Extensin Analogs Cross-linked in Vitro

Held

Li²,

Kamyab³

et al. 2004

Journal of Biological Chemistry

107

129

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“…Transgenic tomato plants were produced by using standard Agrobacterium-mediated plant transformation methods with either neomycin phosphotransferase for kanamycin resistance (LeETR4 antisense constructs) or 5-enolpyruvylshikimate-3-phosphate synthase for glyphosate resistance (NR antisense constructs) as a selectable marker (21). Full-length LeETR4 or NR cDNAs were introduced in their antisense orientations behind the figwort mosaic virus 35S promoter (22) and followed by the nopaline synthase 3Ј terminator.…”

Section: Methodsmentioning

confidence: 99%

The tomato ethylene receptors NR and LeETR4 are negative regulators of ethylene response and exhibit functional compensation within a multigene family

Tieman

Taylor

Ciardi

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

352

202

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The plant hormone ethylene is involved in many developmental processes, including fruit ripening, abscission, senescence, and leaf epinasty. Tomato contains a family of ethylene receptors, designated LeETR1, LeETR2, NR, LeETR4, and LeETR5, with homology to the Arabidopsis ETR1 ethylene receptor. Transgenic plants with reduced LeETR4 gene expression display multiple symptoms of extreme ethylene sensitivity, including severe epinasty, enhanced flower senescence, and accelerated fruit ripening. Therefore, LeETR4 is a negative regulator of ethylene responses. Reduced expression of this single gene affects multiple developmental processes in tomato, whereas in Arabidopsis multiple ethylene receptors must be inactivated to increase ethylene response. Transgenic lines with reduced NR mRNA levels exhibit normal ethylene sensitivity but elevated levels of LeETR4 mRNA, indicating a functional compensation of LeETR4 for reduced NR expression. Overexpression of NR in lines with lowered LeETR4 gene expression eliminates the ethylene-sensitive phenotype, indicating that despite marked differences in structure these ethylene receptors are functionally redundant.

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“…After verification of the inserts, an LR reaction was performed to recombine the fragments into the binary RNAi vector pK7GWIWG2 (Karimi et al, 2002). The resulting vectors were transformed into Agrobacterium tumefaciens strain EHA105 using freeze-thaw transformation (Chen et al, 1994) and transformed to MT wild-type plants by cocultivation with 5-d-old cotyledon explants without a feeding layer, according to a protocol modified from McCormick et al (1986).…”

Section: Generation Of Ful1 and Ful2 Silenced Plantsmentioning

confidence: 99%

The Tomato FRUITFULL Homologs TDR4/FUL1 and MBP7/FUL2 Regulate Ethylene-Independent Aspects of Fruit Ripening

Bemer

Karlova

Ballester³

et al. 2012

Plant Cell

297

276

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Tomato (Solanum lycopersicum) contains two close homologs of the Arabidopsis thaliana MADS domain transcription factor FRUITFULL (FUL), FUL1 (previously called TDR4) and FUL2 (previously MBP7). Both proteins interact with the ripening regulator RIPENING INHIBITOR (RIN) and are expressed during fruit ripening. To elucidate their function in tomato, we characterized single and double FUL1 and FUL2 knockdown lines. Whereas the single lines only showed very mild alterations in fruit pigmentation, the double silenced lines exhibited an orange-ripe fruit phenotype due to highly reduced lycopene levels, suggesting that FUL1 and FUL2 have a redundant function in fruit ripening. More detailed analyses of the phenotype, transcriptome, and metabolome of the fruits silenced for both FUL1 and FUL2 suggest that the genes are involved in cell wall modification, the production of cuticle components and volatiles, and glutamic acid (Glu) accumulation. Glu is responsible for the characteristic umami taste of the present-day cultivated tomato fruit. In contrast with previously identified ripening regulators, FUL1 and FUL2 do not regulate ethylene biosynthesis but influence ripening in an ethylene-independent manner. Our data combined with those of others suggest that FUL1/2 and TOMATO AGAMOUS-LIKE1 regulate different subsets of the known RIN targets, probably in a protein complex with the latter.

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Leaf disc transformation of cultivated tomato (L. esculentum) using Agrobacterium tumefaciens

Cited by 507 publications

References 14 publications

Di-isodityrosine Is the Intermolecular Cross-link of Isodityrosine-rich Extensin Analogs Cross-linked in Vitro

Di-isodityrosine Is the Intermolecular Cross-link of Isodityrosine-rich Extensin Analogs Cross-linked in Vitro

The tomato ethylene receptors NR and LeETR4 are negative regulators of ethylene response and exhibit functional compensation within a multigene family

The Tomato FRUITFULL Homologs TDR4/FUL1 and MBP7/FUL2 Regulate Ethylene-Independent Aspects of Fruit Ripening

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