Structure of a replication-terminator protein complexed with DNA
- 1 October 1996
- journal article
- Published by Springer Nature in Nature
- Vol. 383 (6601) , 598-603
- https://doi.org/10.1038/383598a0
Abstract
The crystal structure of the Escherichia coli replication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 A resolution. The Tus protein folds into a previously undescribed architecture divided into two domains by a central basic cleft. This cleft accommodates locally deformed B-form Ter DNA and makes extensive contacts with the major groove, mainly through two interdomain beta-strands. The unusual structural features of this complex may explain how the replication fork is halted in only one direction.Keywords
This publication has 39 references indexed in Scilit:
- Replication arrestCell, 1995
- Replication fork barriers in the Xenopus rDNANucleic Acids Research, 1994
- Initiation and termination of DNA replication in human rRNA genes.Molecular and Cellular Biology, 1993
- ARREST OF BACTERIAL DNA REPLICATIONAnnual Review of Microbiology, 1992
- Escherichia coli replication terminator protein impedes simian virus 40 (SV40) DNA replication fork movement and SV40 large tumor antigen helicase activity in vitro at a prokaryotic terminus sequence.Proceedings of the National Academy of Sciences, 1991
- DNA-protein interaction at the replication termini of plasmid R6K.Genes & Development, 1991
- Escherichia coli replication termination protein impedes the action of helicases.Proceedings of the National Academy of Sciences, 1989
- The replication terminator protein of E. coli is a DNA sequence-specific contra-helicaseCell, 1989
- A replication fork barrier at the 3′ end of yeast ribosomal RNA genesCell, 1988
- Impediment to replication fork movement in the terminus region of the Bacillus subtilis chromosomeJournal of Molecular Biology, 1984