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Published on October 24, 2008; 10.1104/pp.108.125559

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Received July 1, 2008
Accepted October 22, 2008

Transforming a fructan:fructan 6G-fructosyltransferase from perennial ryegrass (Lolium perenne) into a sucrose:sucrose 1-fructosyltransferase

Bertrand Lasseur , Lindsey Schroeven , Willem Lammens , Katrien Le Roy , German Spangenberg , Helene Manduzio , Rudy Vergauwen , Jeremy Lothier , Marie-Pascale Prud'homme , and Wim Van den Ende *

K.U.Leuven, Laboratorium voor Moleculaire Plantenfysiologie, Kasteelpark Arenberg 31, bus 2434, B-3001 Leuven, Belgium; UMR INRA UCBN 950 EVA, Ecophysiologie Vegetale, Agronomie et nutritions NCS, Universite de Caen, Esplanade de la Paix, 14032 Caen Cedex, France; Department of Primary Industries, Victorian AgriBiosciences Centre, La Trobe R&D Park, Bundoora, Victoria 3083, Australia; CNRS UMR 6037 IFRMP 23, UFR des SCIENCES, Universite de Rouen, 76821 Mont St Aignan, France

* Corresponding author; email: wim.vandenende{at}bio.kuleuven.be.

Fructosyltransferases (FTs) synthesize fructans, fructose polymers accumulating in economically important cool-season grasses and cereals. FTs might be crucial for plant survival under stress conditions in species where fructans represent the major form of reserve carbohydrate, such as in perennial ryegrass (Lolium perenne).

Two FT types can be distinguished: those using sucrose (S-type enzymes: 1-SST, 6-SFT) and those using fructans as preferential donor substrate (F-type enzymes: 1-FFT, 6G-FFT). Here, we report for the first time the transformation of an F-type enzyme (6G-FFT/1-FFT) into an S-type enzyme (1-SST) by using perennial ryegrass 6G-FFT/1-FFT (Lp6G-FFT) and 1-SST (Lp1-SST) as model enzymes. This transformation was accomplished by mutating three amino-acids (N340D, W343R, S415N) in the vicinity of the active site of Lp6G-FFT/1-FFT. In addition, effects of each amino-acid mutation alone or in combination have been studied. Our results strongly suggest that the amino-acid at position 343 (W or R) can greatly determine the donor substrate characteristics by influencing the position of the amino-acid at position 340. Moreover, the presence of R343 negatively affects the formation of neo-fructan type linkages.

The results are compared with recent findings on donor substrate selectivity within the group of plant cell wall invertases and fructan exohydrolases. Taken together, these insights contribute to our knowledge on structure/function relationships within plant family 32 glycosyl hydrolases and open the way to the production of tailor-made fructans at a larger scale.




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