4.5 Article

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

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FEBS LETTERS
卷 468, 期 1, 页码 15-18

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ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01186-8

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

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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.

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