User:Bianca Varney/Replication Terminator Protein: Difference between revisions
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<Structure load='try2' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='try2' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
Replication Terminator Protein (RTP) binds bacterial DNA at Termination (Ter) sites that lie opposite the origin of replication (OriC). When the replication forks meet with RTP, which bound to Ter sites, replication is arrested, and DNA polymerase falls off the bacterial chromosome. However, RTP-Ter interactions are orientation specific, and will only arrest the replication forks traveling in on one direction; either clockwise or anticlockwise once each fork has copied more than half the bacterial chromosome. This permits the entire bacterial chromosome to be copied. | Replication Terminator Protein (RTP) arrests replication in bacteria. RTP binds bacterial DNA at Termination (Ter) sites that lie opposite the origin of replication (OriC). When the replication forks meet with RTP, which bound to Ter sites, replication is arrested, and DNA polymerase falls off the bacterial chromosome. However, RTP-Ter interactions are orientation specific, and will only arrest the replication forks traveling in on one direction; either clockwise or anticlockwise once each fork has copied more than half the bacterial chromosome. This permits the entire bacterial chromosome to be copied. | ||
==Mechanism== | ==Mechanism== | ||
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[[Image:Ter sites.png]] | [[Image:Ter sites.png]] | ||
==Biological Role== | |||
==Structure== | ==Structure== | ||
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The RTP is organized into a dimer by the association of their long α helices within the C-terminus. The ‘winged helix’ is believed to be involved as the major DNA-binding domain however two of the α helices, at the centre of the protein, and two β strands, in the outer regions, have been suggested to fit adjacently into the major and minor grooves respectively. The unstructured N terminal region is may also have a role in DNA-binding. This binding interaction is different from the Tus-Ter interactions in ''E. coli''. | The RTP is organized into a dimer by the association of their long α helices within the C-terminus. The ‘winged helix’ is believed to be involved as the major DNA-binding domain however two of the α helices, at the centre of the protein, and two β strands, in the outer regions, have been suggested to fit adjacently into the major and minor grooves respectively. The unstructured N terminal region is may also have a role in DNA-binding. This binding interaction is different from the Tus-Ter interactions in ''E. coli''. | ||
==References== | |||
