User:Nathan Harris/Tus: Difference between revisions

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==='''Tus-DnaB interactions'''===

Numerous studies support a model for replication termination resulting specifically from Tus-DnaB protein interactions.

Experimentation in the field has demonstrated that the E49 within the L1 loop of the non-permissive face of Tus is important in the formation of protein-protein interactions with DnaB. When this glutamic acid is exchanged for lysine (E49K), an increase in affinity for ''Ter'' and a decrease in affinity for DnaB result. Despite the increased affinity for ''Ter'', this E49K mutatation results in a reduced capability of polar replication fork termination demonstrating the importance of Tus-DnaB interactions.

Experimentation in the field has demonstrated that the <scene name='User:Nathan_Harris/Tus/E49/1'>E49</scene> within the L1 loop of the non-permissive face of Tus is important in the formation of protein-protein interactions with DnaB. When this glutamic acid is exchanged for lysine (E49K), an increase in affinity for ''Ter'' and a decrease in affinity for DnaB result. Despite the increased affinity for ''Ter'', this E49K mutatation results in a reduced capability of polar replication fork termination demonstrating the importance of Tus-DnaB interactions.

In further confirmation of this helicase specific mechanism, the engineering of intra-strand covalent crosslinks introduced immediately upstream of the C6 of ''Ter'' prevent DnaB helicase from unwinding the C6. Despite this inability to unwind and from a locked complex with ''Tus'', polar fork termination is still permitted indicating that the formation of a locked complex is unnecessary for replication termination.

@@ Line 44: / Line 44: @@
 ==='''Tus-DnaB interactions'''===
 Numerous studies support a model for replication termination resulting specifically from Tus-DnaB protein interactions.
-Experimentation in the field has demonstrated that the E49 within the L1 loop of the non-permissive face of Tus is important in the formation of protein-protein interactions with DnaB. When this glutamic acid is exchanged for lysine (E49K), an increase in affinity for ''Ter'' and a decrease in affinity for DnaB result. Despite the increased affinity for ''Ter'', this E49K mutatation results in a reduced capability of polar replication fork termination demonstrating the importance of Tus-DnaB interactions.
+Experimentation in the field has demonstrated that the <scene name='User:Nathan_Harris/Tus/E49/1'>E49</scene> within the L1 loop of the non-permissive face of Tus is important in the formation of protein-protein interactions with DnaB. When this glutamic acid is exchanged for lysine (E49K), an increase in affinity for ''Ter'' and a decrease in affinity for DnaB result. Despite the increased affinity for ''Ter'', this E49K mutatation results in a reduced capability of polar replication fork termination demonstrating the importance of Tus-DnaB interactions.
 In further confirmation of this helicase specific mechanism, the engineering of intra-strand covalent crosslinks introduced immediately upstream of the C6 of ''Ter'' prevent DnaB helicase from unwinding the C6. Despite this inability to unwind and from a locked complex with ''Tus'', polar fork termination is still permitted indicating that the formation of a locked complex is unnecessary for replication termination.