THE PLANT CELL, Vol 1, Issue 5 493-499, Copyright © 1989 by American Society of Plant Biologists
Identification, Isolation, and N-Terminal Sequencing of Style Glycoproteins Associated with Self-Incompatibility in Nicotiana alata
W. Jahnen, M. P. Batterham, A. E. Clarke, R. L. Moritz and R. J. Simpson
Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia
S-Gene-associated glycoproteins (S-glycoproteins) from styles of Nicotiana
alata, identified by non-equilibrium two-dimensional electrophoresis, were
purified by cation exchange fast protein liquid chromatography with yields
of 0.5 to 8 micrograms of protein per style, depending on the S-genotype of
the plant. The method relies on the highly basic nature of the
S-glycoproteins. The elution profiles of the different S-glycoproteins from
the fast protein liquid chromatography column were characteristic of each
S-glycoprotein, and could be used to establish the S-genotype of plants in
outbreeding populations. In all cases, the S-genotype predicted from the
style protein profile corresponded to that predicted from DNA gel blot
analysis using S-allele-specific DNA probes and to that established by
conventional breeding tests. Amino-terminal sequences of five purified
S-glycoproteins showed a high degree of homology with the previously
published sequences of N. alata and Lycopersicon esculentum
S-glycoproteins.
