A Single Nuclease Active Site of the Escherichia coli RecBCD Enzyme Catalyzes Single-stranded DNA Degradation in Both Directions

• Published in: The Journal of biological chemistry Vol. 275; no. 1; pp. 507 - 513
• Main Authors: Wang, Jingdi, Chen, Ruiwu, Julin, Douglas A.
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 07.01.2000
• Subjects: Amino Acid Sequence; Catalytic Domain; DNA damage; DNA Helicases - genetics; DNA Helicases - metabolism; DNA, Bacterial - metabolism; DNA, Single-Stranded - metabolism; Escherichia coli; Escherichia coli - enzymology; Escherichia coli Proteins; Exodeoxyribonuclease V; Exodeoxyribonucleases - genetics; Exodeoxyribonucleases - metabolism; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; RecBCD enzyme; Sequence Homology, Amino Acid

The RecBCD enzyme of Escherichia coli is an ATP-dependent DNA exonuclease and a helicase. Its exonuclease activity is subject to regulation by an octameric nucleotide sequence called χ. In this study, site-directed mutations were made in the carboxyl-terminal nuclease domain of the RecB subunit, an...