User:Chloe Paul/Replication Terminator Protein: Difference between revisions

<StructureSection load='2efw' size='300' side='right' caption='RTP bound to native DNA (PDB entry [[2efw]])' scene='User:Chloe_Paul/Replication_Terminator_Protein/Rtpasym/1'>The RTP:DNA interaction has been shown to be able to induce two different conformations of RTP depending upon the nature of the DNA. Early experiments used to determine how they interacted, used symmetric DNA (sDNA) which resulted in RTP binding symmetrically. However in nature, RTP was found to have a polar mechanism which implied asymetric binding, leading to further investigations of how RTP bound to DNA. It was later shown that when RTP bound to native or non-symmetric DNA (nDNA) it induced an asymmetric "wing-up, wing-down" form of RTP with a two faces. One face, known as the “blocking” face acts to terminate the approaching replication fork. The other face is described as the “permissive” face as it allows the replication fork to proceed along the DNA.  These faces correspond to the A site and B site of the Ter sequence of DNA respectively. These DNA sites are the two halves of the pseudosymmetric palindromic sequence. The conformation and thus function of the RTP monomer depends on which site the RTP monomer binds to.  It is the concept of these two faces that give rise to the polar mechanism of RTP.</StructureSection>