Rapid stalk elongation in tulip (Tulipa gesneriana L. cv. Apeldoorn) and the combined action of cold-induced invertase and the water-channel protein gammaTIP.
Many bulbous plants need a low-temperature treatment for flowering. Cold, for example, affects the elongation of the stalk, thereby influencing the quality of the cut flower. How the elongation of the stalk is promoted by cold and which physiological and biochemical mechanisms are involved have remained obscure. As invertase has been shown to be involved in the cold-induced elongation of the flower stalks of tulips (Lambrechts et al., 1994, Plant Physiol 104: 515-520), we further characterized this enzyme by cloning the cDNA and analysing its expression in various tissues of the tulip (Tulipa gesneriana L. cv. Apeldoorn) stalk. In addition, the role of sucrose synthase was investigated. Since turgor pressure is an important force driving cell elongation, the role of a water-channel protein (gammaTIP) was studied in relation to these two enzymes. The mRNA level of the invertase found was substantially up-regulated as a result of cold treatment. Analysis of the amino acid sequence of this invertase revealed the presence of a vacuolar targeting signal. Two different forms of sucrose synthase were found, the expression of one of them appeared to be restricted to the vascular tissue while the other form was present in the surrounding tissue. Both sucrose synthases were present in the stalk during the entire period of bulb storage and after planting, but their activities declined during stalk elongation. The expression of the gammaTIP gene was restricted mainly to the vascular tissue and its expression profile was identical to that of invertase. Simultaneous expression of invertase and gammaTIP possibly leads to an increase in osmotic potential and vacuolar water uptake, thus providing a driving force for stretching the stalk cells.
Balk
P A
PA
Agrotechnological Research Institute, Department of Molecular Regulation and Plant Quality, Bornsesteeg 59, P.O. Box 17, 6700 AA Wageningen, The Netherlands.
de Boer
A D
AD
D000595:Amino Acid Sequence; D020346:Aquaporins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D003001:Cloning, Molecular; D003080:Cold Temperature; D018744:DNA, Plant; D004789:Enzyme Activation; D015870:Gene Expression; D005964:Glucosyltransferases / Q000235:genetics / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000235:genetics / Q000378:metabolism*; D019668:Liliaceae / Q000201:enzymology* / Q000254:growth & development; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D018272:Porins; D017386:Sequence Homology, Amino Acid; D013997:Time Factors; D043324:beta-Fructofuranosidase
D020346:Aquaporins; D018744:DNA, Plant; D008565:Membrane Proteins; D010940:Plant Proteins; D018272:Porins; C091845:gamma-TIP protein, plant; D005964:Glucosyltransferases; C022699:sucrose synthase; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase