Pollen UDP-glucose pyrophosphorylase showing polymorphism well-correlated to the S genotype of Pyrus pyrifolia

A polymorphic protein well-correlated to the diploid S genotypes of the pollen parent was detected by two-dimensional gel electrophoresis in Pyrus pyrifolia (Japanese pear). Its molecular weight was about 50 kDa, and it was expressed primarily in pollen. Partial amino acid sequences of the polymorphic protein from 'Nijisseiki' (S2S4), a cultivar of P. pyrifolia, were determined. Based on these sequences, two cDNA sequences associated with the S2 and S4 genotypes were identified by PCR-based methods. Both encode a protein of 458 amino acids whose sequence has high similarity to eukaryotic UDP-glucose pyrophosphorylases (UGPases) (EC 2.7.7.9), so they were named UGPases PA and PC. As there are only three amino acid substitutions between UGPases PA and PC, it is unlikely that they are pollen factors that recognize self and non-self S-RNases. Although this UGPase had more than 75% sequence identity to the known plant UGPases, its C-terminal sequences differed markedly. This unique C-terminal region of UGPases PA and PC may act in their subcellular localization in the pollen or interact with some other factor(s).