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Protease activity of CND41, a chloroplast nucleoid DNA‐binding protein, isolated from cultured tobacco cells
Author(s) -
Murakami Shinya,
Kondo Yoshihiko,
Nakano Takeshi,
Sato Fumihiko
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01186-8
Subject(s) - biochemistry , protease , dna , nucleoid , sodium dodecyl sulfate , chloroplast , biology , chemistry , microbiology and biotechnology , escherichia coli , enzyme , gene
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, Fe 3+ and sodium dodecyl sulfate.