The DNA Binding Characteristics of the Trimeric EcoKI Methyltransferase and its Partially Assembled Dimeric Form Determined by Fluorescence Polarisation and DNA Footprinting

• Published in: Journal of molecular biology Vol. 283; no. 5; pp. 947 - 961
• Main Authors: Powell, Lynn M, Connolly, Bernard A, Dryden, David T.F
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 13.11.1998
• Subjects: Base Sequence; Binding Sites - genetics; Dimerization; DNA - chemistry; DNA - genetics; DNA - metabolism; DNA binding; DNA Footprinting; DNA Methylation; DNA methyltransferase; DNA Restriction Enzymes - chemistry; DNA Restriction Enzymes - metabolism; Escherichia coli; Escherichia coli - enzymology; fluorescence anisotropy; Fluorescence Polarization; Fluorescent Dyes; hexachlorofluorescein; Multienzyme Complexes - chemistry; Multienzyme Complexes - metabolism; Nucleic Acid Conformation; Oligodeoxyribonucleotides - chemistry; Oligodeoxyribonucleotides - metabolism; Protein Conformation; S-Adenosylmethionine - metabolism; Site-Specific DNA-Methyltransferase (Adenine-Specific) - chemistry; Site-Specific DNA-Methyltransferase (Adenine-Specific) - metabolism; Substrate Specificity; UV; fluorescence anisotropy; TBE; hsd; DNA methyltransferase; hexachlorofluorescein; DNase I; DNA footprinting; DNA binding; bp; K d; AdoMet

The type I DNA restriction and modification systems of enteric bacteria display several enzymatic activities due to their oligomeric structure. Partially assembled forms of the EcoKI enzyme from E. coli K12 can display specific DNA binding properties and modification methyltransferase activity. The...