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

FEBS Lett. 2000 Feb 18;468(1):15-8. doi: 10.1016/s0014-5793(00)01186-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Cells, Cultured
  • DNA / pharmacology
  • DNA, Chloroplast / metabolism*
  • DNA-Binding Proteins / isolation & purification
  • DNA-Binding Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Endopeptidases / isolation & purification
  • Endopeptidases / metabolism*
  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / pharmacology
  • Ferric Compounds / pharmacology
  • Hemoglobins / metabolism
  • Hydrogen-Ion Concentration
  • NADP / metabolism
  • Pepsin A / metabolism
  • Pepstatins / pharmacology
  • Plant Proteins / isolation & purification
  • Plant Proteins / metabolism
  • Plants, Toxic*
  • RNA / pharmacology
  • Sequence Analysis
  • Tobacco / cytology
  • Tobacco / enzymology*

Substances

  • CND41 protein, Nicotiana tabacum
  • DNA, Chloroplast
  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • Ferric Compounds
  • Hemoglobins
  • Pepstatins
  • Plant Proteins
  • NADP
  • RNA
  • Adenosine Triphosphate
  • DNA
  • Endopeptidases
  • Pepsin A