Structural and enzymatic properties of an in vivo proteolytic form of PD-S2, type 1 ribosome-inactivating protein from seeds of Phytolacca dioica L

被引:6
|
作者
Di Maro, Antimo [1 ]
Berisio, Rita [2 ]
Ruggiero, Alessia [2 ]
Tamburino, Rachele [1 ]
Severino, Valeria [1 ]
Zacchia, Enza [1 ]
Parente, Augusto [1 ]
机构
[1] Univ Naples 2, Dipartimento Sci Vita, I-81100 Caserta, Italy
[2] CNR, Ist Biostrut & Bioimmagini, I-80134 Naples, Italy
关键词
3D modeling; Circular dichroic spectroscopy; Proteolytic regulation; Phytolacca dioica; Ribosome-inactivating proteins; GLYCOSIDASE ACTIVITY; LEAVES; PLANTS; EXPRESSION; LEGUMAINS; DNA;
D O I
10.1016/j.bbrc.2012.04.036
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
PD-S2, type 1 ribosome-inactivating protein from Phytolacca dioica L seeds, is an N-beta-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. (C) 2012 Elsevier Inc. All rights reserved.
引用
收藏
页码:514 / 520
页数:7
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