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

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2012年 / 421卷 / 03期

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

页码：514 / 520

页数：7