Germins and germin-like proteins (GLPs) comprise large families of extracellular plant glycoproteins that are structurally similar, yet they have been reported to have distinct biochemical activities: oxalate oxidase and superoxide dismutase activities, respectively. We expressed an azalea GLP (RmGLP2) in cultured cells of tobacco, and determined that the extracellular protein fraction and the recombinant RmGLP2 protein purified from these cells catalyzed the oxidation of oxalate. Notably, this activity is purportedly restricted to germin and has not been demonstrated for a GLP. Although the specific activity of the purified RmGLP2 protein was low compared with that of a previously characterized barley germin/oxalate oxidase, tobacco cells expressing RmGLP2 exhibited significantly reduced oxalate levels. Thus, RmGLP2 represents the first reported GLP with oxalate oxidase activity.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Mar 13 2015|
Bibliographical noteFunding Information:
This work was supported in part by Grants-in-Aid for Scientific Research on Innovative Areas (grant nos. 23119514 and 25119717 to A.S.) from the Ministry of Education, Culture, Sports, Science and Technology of Japan .
© 2015 Elsevier Inc. All rights reserved.
- Extracellular matrix protein
- Germin-like protein
- Hydrogen peroxide
- Oxalate oxidase
- Superoxide dismutase