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 i...

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Veröffentlicht in:	Plant molecular biology 1990-09, Vol.15 (3), p.457-464
Hauptverfasser:	Cannon, G.C, Heinhorst, S
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - isolation & purification Adenosine Triphosphate - physiology adenosinetriphosphatase Base Sequence Biological and medical sciences Biotechnology chloroplasts Chloroplasts - enzymology DNA DNA Helicases - isolation & purification DNA Replication enzyme activity Enzyme engineering enzymes Fundamental and applied biological sciences. Psychology Glycine max Glycine max - enzymology Improved methods for extraction and purification of enzymes magnesium Magnesium - physiology manganese Manganese - physiology Methods. Procedures. Technologies Molecular Sequence Data Plant Proteins - isolation & purification purification requirements Substrate Specificity
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Zusammenfassung:	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.
ISSN:	0167-4412 1573-5028
DOI:	10.1007/BF00019162