Protease activity of CND41, a chloroplast nucleoid DNA-binding protein, isolated from cultured tobacco cells

被引：70

作者：

Murakami, S

Kondo, Y

Nakano, T

Sato, F ^{[1
]}

机构：

[1] RIKEN, Inst Phys & Chem Res, Wako, Saitama 3510189, Japan

[2] Kyoto Univ, Grad Sch Biostudies, Dept Plant Gene & Totipotency, Kyoto 6068502, Japan

[3] Kyoto Univ, Grad Sch Agr, Dept Appl Life Sci, Kyoto 6068502, Japan

来源：

FEBS LETTERS | 2000年 / 468卷 / 01期

关键词：

chloroplast nucleoid; DNA-binding protein; aspartic protease; Nicotiana tabacum;

D O I：

10.1016/S0014-5793(00)01186-8

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：

CND41 is a 41 kDa DNA-binding protein isolated from chloroplast nucleoids of cultured tobacco cells. The presence of the active domain of aspartic protease in the deduced amino acid sequence of CND41 suggests that it has proteolytic activity. To confirm this, CND41 was highly purified from cultured tobacco cells and its proteolytic activity was characterized with fluorescein isothiocyanate-labeled hemoglobin as the substrate. The purified CND41 had strong proteolytic activity at an acidic pH (pH 2-4). This activity was inhibited by various chemicals, including the nucleoside triphosphates, NADPH, Fe3+ and sodium dodecyl sulfate. (C) 2000 Federation of European Biochemical Societies.

引用

页码：15 / 18

页数：4

共 18 条

[1] Protein stability and degradation in chloroplasts [J].