Cloning of a cDNA for a chitinase homologue which lacks chitin-binding sites and is down-regulated by water stress and wounding
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Benhamou N, Asselin A: Attempted localization of a substrate for chitinases in plant cells reveals abundant N-acetyl-D-glucosamine residues in secondary walls. Biol Cell 67: 341?350 (1989).
Boller T: Ethylene and the regulation of antifungal hydrolases in plants. In: Miflin BJ (ed) Surveys of Plant Molecular Biology and cell Biology, vol 5, pp. 145?174, Oxford University Press, Oxford (1988).
Broglie KE, Gaynor JJ, Broglie RM: Ethylene-regulated gene expression: Molecular cloning of the genes encoding an endochitinase fromPhaseolus vulgaris. Proc Natl Acad Sci USA 83: 6820?6824 (1986).
Cairney J, Chang S, Dias D, Funkhouser EA, Newton RJ: cDNA cloning and analysis of loblolly pine genes induced by drought stress. In: Proceedings, 22nd Southern Forest Tree Improvement Conference, 14?17 June, Atlanta, Georgia, pp. 357?369 (1993).
Chang S, Puryear J, Cairney J: A simple and efficient method for isolating RNA from pine trees. Plant Mol Biol 11: 114?117 (1993).
Chrispeels MJ, Raikhel NV: Lectins, lectin genes and their role in plant defense. Plant Cell 3: 1?9 (1991).
Collinge DB, Kragh KM, Mikkelsen JD, Nielsen KK, Rasmussen U, Vad K: Plant chitinases. Plant J 3: 31?40 (1993).
De Jong AJ, Cordewener J, Schiavo FL, Terzi M, Vandekerckhove J, van Kammen A, de Vries SC: A carrotsomatic embryo mutant is rescued by chitinase. Plant Cell 4: 425?433 (1992).
de Jong AJ, Heidstra R, Spaink HP, Hartog MV, Meijer EA, Hendriks T, Schiavo FL, Terzi M, Bisseling T, van Kammen A, de Vries SC:Rhizobium lipooligosaccharides rescue a carrot somatic embryo mutant. Plant Cell 5: 615?620 (1993).
Dénarié J, Cullimore J: Lipo-oligosaccharide nodulation factors: a minireview. New class of signalling molecules mediating recognition and morphogenesis. Cell 74: 951?954 (1993).
Deshusses J, Belet M: Purification and properties of the myoinositol-binding protein from aPseudomonas sp. J Bact 159: 179?183 (1984).
Fütterer J, Kiss-László Z, Hohn T: Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA. Cell 73: 789?802 (1993).
Gallie DR: Posttranscriptional regulation of gene expression in plants. Annu Rev Plant Physiol Plant Mol Biol 44: 77?105 (1993).
Gauchat-Feiss D, Frey J, Belet M, Deshusses J: Cloning of genes involved in myo-inositol transport in aPseudomonas sp. J Bact 162: 324?327 (1984).
Geballe AP, Morris DR: Initiation codons with 5?-leaders of mRNAs as regulators of translation. Trends Biochem Sci 19: 159?164 (1994).
Hejgaard J, Jacobsen S, Bjørn SE, Kragh KM: Antifungal activity of chitin-binding PR-4 proteins from barley grain and stressed leaf. FEBS Lett 307: 389?392 (1992).
Hentze MW, Caughman SW, Sasey JL, Kowller DM, Raouault TA, Harjord JB, Klausner RD: A model for the structure and function of iron-responsive elements. Gene 72: 201?208 (1988).
Iseli B, Boller T, Neuhaus J-M: The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol 103: 221?226 (1993).
Joshi CP: An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucl Acids Res 16: 6643?6653 (1987).
Melefors O, Hentze MW: Translational regulation by mRNA/protein interactions in eukaryotic cells: ferritin and beyond. BioEssays 15: 85?90 (1993).
Neale AD, Wahleithner FA, Lund M, Bonnett HT, Kelly A, Meeks-Wagner DR, Peacock WJ, Dennis ES: Chitinase, ?-1?3-glucanase, osmotin and extensin are expressed in tobacco explants during flower formation. Plant Cell 2: 673?684 (1990).
Parsons TJ, Bradshaw HD, Gordon MP: Systemic accumulation of specific mRNAs in response to wounding in poplar trees. Proc Natl Acad Sci USA 86: 7895?7899 (1989).
Raikhel NV, Lee H-I, Broekaert WF: Structure and function of chitin-binding proteins. Annu Rev Plant Physiol Plant Mol Biol 44: 591?615 (1993).
Roche P, Debellé F, Maillet F, Lerouge P, Faucher C, Truchet G, Dénarié J, Promé JC, Molecular basis of symbiotic host specificity inRhizobium meliloti: nodH andnodPQ genes encode the sulfation of lipo-oligosaccharide signals. Cell 67: 1131?1143 (1991).
Shultze M, Kondorosi E, Kondorosi A, Staehelin C, Mellor RB, Boller T: The sulfate group on the reducing end protects Nod signals ofR. meliloti against hydrolysis byMedicago chitinases. In: Palacios R, Mora J, Newton W (eds) New Horizons in Nitrogen Fixation, pp. 159?164. Kluwer Academic Publishers, Dordrecht (1993).
Sela-Buurlage MB, Ponstein AS, Bres-Vloemans SA, Melchers LS, van den Elzen FJM, Cornelissen BJC: Only specific tobacco (Nicotiana tabacum) chitinases and ?-1?3-glucanases exhibit anti-fungal activity. Plant Physiol 101: 857?863 (1993).
Shinishi H, Mohnen D, MeinsJr F: Regulation of a plant pathogenesis-related enzyme: Inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc Natl Acad Sci USA 84: 89?93 (1987).
Shinishi H, Neuhaus J-M, Ryals J, MeinsJr F: Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain. Plant Mol Biol 14: 357?368 (1990).