RTP and Tus: Difference between revisions
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4. DnaB engineers a DNA structure on the permissive face that actively promotes Tus dissociation. | 4. DnaB engineers a DNA structure on the permissive face that actively promotes Tus dissociation. | ||
Neylon ''et al'' concluded that the Clamp model was too simplistic to explain the polar nature of fork arrest. They concluded based on mutational data that it is probably a combination of Tus-DnaB interactions as well as Tus-Ter binding strength that contribute to fork-arrest activity. | Neylon ''et al'' concluded that the Clamp model was too simplistic to explain the polar nature of fork arrest. They concluded based on mutational data that it is probably a combination of Tus-DnaB interactions as well as Tus-''Ter'' binding strength that contribute to fork-arrest activity. | ||
'''So how does Tus actually stop the replication fork? And why is it a polar arrest mechanism?''' | '''So how does Tus actually stop the replication fork? And why is it a polar arrest mechanism?''' | ||
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The locked Tus-''Ter'' complex is the most stable known monomeric DNA binding protein with a double-stranded sequence-specific recognition sequence - a half life of 550min has been reported (Mulcair, 2006). The formation of a large hydrogen-bond network is critical to sequence recognition and the stability of the twisted β-strands lying across the major groove. | The locked Tus-''Ter'' complex is the most stable known monomeric DNA binding protein with a double-stranded sequence-specific recognition sequence - a half life of 550min has been reported (Mulcair, 2006). The formation of a large hydrogen-bond network is critical to sequence recognition and the stability of the twisted β-strands lying across the major groove. | ||
'''When we thought we had a nice, elegant theory, someone had to come screw it all up.''' | |||