Partial purification and characterization of a DNA helicase from chloroplasts of Glycine max.
A DNA helicase activity was detected in extracts of purified chloroplasts from the SB-1 cell line of Glycine max and partially purified by column chromatography on DEAE cellulose, phosphocellulose, and single-stranded DNA cellulose. The chloroplast helicase has a DNA-dependent ATPase activity, and its strand displacement activity is strictly dependent upon the presence of a nucleoside triphosphate and Mg2+ or Mn2+. Strand displacement activity does not require a free unannealed single-strand or replication fork-like structure.
Cannon
G C
GC
Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg 39406.
Heinhorst
S
S
D000251:Adenosine Triphosphatases / Q000302:isolation & purification; D000255:Adenosine Triphosphate / Q000502:physiology; D001483:Base Sequence; D002736:Chloroplasts / Q000201:enzymology*; D004265:DNA Helicases / Q000302:isolation & purification*; D004261:DNA Replication; D008274:Magnesium / Q000502:physiology; D008345:Manganese / Q000502:physiology; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000302:isolation & purification*; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity
D010940:Plant Proteins; D008345:Manganese; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D004265:DNA Helicases; D008274:Magnesium