A tale of two terminators: crystal structures sharpen the debate on DNA replication fork arrest mechanisms.
The structure of the Tus-Ter DNA replication fork arrest complex of Escherichia coli reveals a novel architecture for the bound Tus protein and a new type of DNA-binding motif. The structure of the complex may explain how Tus can block movement of a replication fork approaching from one direction and not the other.
Wake
R
R
Department of Biochemistry, University of Sydney, NSW 2006, Australia. g.wake@biochem.usyd.edu.au.
King
G
G
D001412:Bacillus subtilis / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry*; D004261:DNA Replication / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D001426:Bacterial Proteins; C062011:DNA replication terminus site-binding protein, E coli; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C063112:rtP protein, Bacillus subtilis; C061910:tus protein, Bacteria; C489236:tus protein, E coli