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EnglishPD-S2, type 1 ribosome-inactivating protein from Phytolacca dioica L. seeds, is an N-β-glycosidase likely involved in plant defence. In this work, we purified and characterized an in vivo proteolytic form of PD-S2, named cutPD-S2. Spectroscopic characterization of cutPD-S2 showed that the proteolytic cleavage between Asn195 and Arg196 does not alter the protein fold, but significantly affects its thermal stability. Most importantly, the proteolytic cleavage induces a 370-fold decrease of PD-S2 capacity of inhibiting in vitro protein biosynthesis.Our data catch the turning point from a typical role of PD-S2 as a defence protein to that of supplier of essential amino acids during seedling development. © 2012 Elsevier Inc.
| Titolo: | Structural and enzymatic properties of an in vivo proteolytic form of PD-S2, type 1 ribosome-inactivating protein from seeds of Phytolacca dioica L | |
| Autori: | ||
| Data di pubblicazione: | 2012 | |
| Rivista: | ||
| Abstract: | PD-S2, type 1 ribosome-inactivating protein from Phytolacca dioica L. seeds, is an N-β-glycosidase likely involved in plant defence. In this work, we purified and characterized an in vivo proteolytic form of PD-S2, named cutPD-S2. Spectroscopic characterization of cutPD-S2 showed that the proteolytic cleavage between Asn195 and Arg196 does not alter the protein fold, but significantly affects its thermal stability. Most importantly, the proteolytic cleavage induces a 370-fold decrease of PD-S2 capacity of inhibiting in vitro protein biosynthesis.Our data catch the turning point from a typical role of PD-S2 as a defence protein to that of supplier of essential amino acids during seedling development. © 2012 Elsevier Inc. | |
| Handle: | http://hdl.handle.net/11591/186365 | |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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