Structure-specific DNA nucleases: structural basis for 3D-scissors.
Structure-specific DNA nucleases play important roles in various DNA transactions such as DNA replication, repair and recombination. These enzymes recognize loops and branched DNA structures. Recent structural studies have provided detailed insights into the functions of these enzymes. Structures of Holliday junction resolvase revealed that nucleases are broadly diverged in the way in which they fold, however, are required to form homodimers with large basic patches of protein surfaces, which are complementary to DNA tertiary structures. Many nucleases maintain structure-specific recognition modes, which involve particular domain arrangements through conformal changes of flexible loops or have a separate DNA binding domain. Nucleases, such as FEN-1 and archaeal XPF, are bound to proliferating cell nuclear antigen through a common motif, and thereby actualize their inherent activities.
Nishino
Tatsuya
T
Biomolecular Engineering Research Institute (BERI), 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.
Ishino
Yoshizumi
Y
Morikawa
Kosuke
K
D001105:Archaea / Q000201:enzymology / Q000235:genetics; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000502:physiology*; D045585:Flap Endonucleases / Q000737:chemistry* / Q000502:physiology*; D045565:Holliday Junction Resolvases / Q000737:chemistry* / Q000502:physiology*
D004268:DNA-Binding Proteins; C095888:xeroderma pigmentosum group F protein; D045585:Flap Endonucleases; D045565:Holliday Junction Resolvases