例如:"lncRNA", "apoptosis", "WRKY"

An asymmetric structure of the Bacillus subtilis replication terminator protein in complex with DNA.

J. Mol. Biol.2007 Jul 13;370(3):481-91. Epub 2007 Mar 02
J P Vivian 1 , C J Porter , J A Wilce , M C J Wilce
J P Vivian 1 , C J Porter , J A Wilce , M C J Wilce

[No authors listed]

Author information
  • 1 Department of Pharmacology, University of Western Australia, Nedlands, Western Australia, 6009, Australia.

摘要


In Bacillus subtilis, the termination of DNA replication via polar fork arrest is effected by a specific protein:DNA complex formed between the replication terminator protein (RTP) and DNA terminator sites. We report the crystal structure of a replication terminator protein homologue (RTP.C110S) of B. subtilis in complex with the high affinity component of one of its cognate DNA termination sites, known as the TerI B-site, refined at 2.5 A resolution. The 21 bp RTP:DNA complex displays marked structural asymmetry in both the homodimeric protein and the DNA. This is in contrast to the previously reported complex formed with a symmetrical TerI B-site homologue. The induced asymmetry is consistent with the complex's solution properties as determined using NMR spectroscopy. Concomitant with this asymmetry is variation in the protein:DNA binding pattern for each of the subunits of the RTP homodimer. It is proposed that the asymmetric "wing" positions, as well as other asymmetrical features of the RTP:DNA complex, are critical for the cooperative binding that underlies the mechanism of polar fork arrest at the complete terminator site.

基因