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- Title
Accumulation of pathogenesis-related (PR) 10/Bet v 1 protein homologues in mulberry ( Morus bombycis Koidz.) tree during winter.
- Authors
Ukaji, N.; Kuwabara, C.; Takezawa, D.; Arakawa, K.; Fujikawa, S.
- Abstract
Seasonal evaluation of total soluble protein fractions extracted from cortical parenchyma cells of mulberry ( Morus bombycis Koidz.) tree identified a predominant 18 kDa protein that was directly correlated to periods of cold acclimation. The 18 kDa protein, designated as WAP18 ( winter accumulating 18 kDa proteins) increased from September to December and then gradually decreased until June. The maximum levels of WAP18 were detected in mid-winter, which corresponds to the maximum freeze tolerance in cortical parenchyma cells of mulberry tree. Two-dimensional gel electrophoresis confirmed that WAP18 consists of at least three proteins that range between an isoelectric point of 5.0 and 6.0. All three proteins reacted with anti-WAP18 antibodies, thereby suggesting that they represent individual isoforms. Furthermore, N-terminal amino acid sequence analysis demonstrated that all three proteins contain high sequence similarity to each other and high homology to pathogenesis-related (PR) −10/Bet v 1 protein families. The purified WAP18 exhibited in vitro cryoprotective activity for the freeze labile l-lactate dehydrogenase (LDH) enzyme. These results suggest that WAP18 may function in the freezing tolerance mechanism of cortical parenchyma cells of mulberry tree during winter.
- Subjects
MULBERRY; PLANT proteins; GEL electrophoresis; HOMOLOGY (Biology); LACTATE dehydrogenase; AMINO acid sequence
- Publication
Plant, Cell & Environment, 2004, Vol 27, Issue 9, p1112
- ISSN
0140-7791
- Publication type
Article
- DOI
10.1111/j.1365-3040.2004.01216.x