Failed expression of an endo-beta-1,4-glucanhydrolase (cellulase) in a non-abscinding mutant of Lupinus angustifolius cv Danja.
Cellulase expressions in a normal shedding wild-type and a non-abscinding single gene mutant of Lupinus angustifolius have been studied during ethylene treatments of leaf abscission zone explants. Of the range of different glycohydrolases investigated only the abscission cell-specific beta-1,4-glucanhydrolase (cellulase) was not produced in the non-abscinding mutant. An endo-polygalacturonase was induced equally in both wild-type and mutant and other glycohydrolases were equally up-regulated. The abscission cell-specific cellulase induced at shedding of wild-type is antigenically similar to the Phaseolus vulgaris induced leaf abscission pI 9.5 cellulase but with a higher molecular mass (50 kD compared with 48 kD) and like the bean abscission-specific cellulase that of lupin is not glycosylated. Causes of the loss of function of cellulase expression in the non-shedding mutant are discussed.
Henderson
J
J
Oxford Research Unit, Open University, Foxcombe Hall, Boars Hill, Oxford, OX1 5HR, UK.
Lyne
L
L
Osborne
D J
DJ
D002480:Cellulase / Q000235:genetics / Q000378:metabolism*; D007887:Fabaceae / Q000201:enzymology* / Q000235:genetics; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000378:metabolism; D007525:Isoelectric Focusing; D009154:Mutation; D011096:Polygalacturonase / Q000378:metabolism; D001617:beta-Glucosidase / Q000378:metabolism
D011096:Polygalacturonase; D001617:beta-Glucosidase; D004693:Glucan Endo-1,3-beta-D-Glucosidase; D002480:Cellulase