RTP and Tus: Difference between revisions

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<Structure load='1ECR' size='400' frame='true' align='right' caption='Tus complexed with Ter DNA (Kamada ''et al'' 1996)' scene='Insert optional scene name here' />
<Structure load='1ECR' size='400' frame='true' align='right' caption='Tus complexed with Ter DNA (Kamada ''et al'' 1996)' scene='Insert optional scene name here' />
<scene name='colorSTRUCTURE'>structure</scene>
<scene name='colorSTRUCTURE'>structure</scene>
{{Template:ColorKey Composition Protein}}, {{Template:ColorKey Composition DNA}}
<Structure load='1F4K' size='400' frame='true' align='left' caption='RTP complexed with ''Ter''I B-site' (Wilce ''et al'' 2001)' scene='Insert optional scene name here' />
<Structure load='1F4K' size='400' frame='true' align='left' caption='RTP complexed with ''Ter''I B-site' (Wilce ''et al'' 2001)' scene='Insert optional scene name here' />
<scene name='colorSTRUCTURE'>structure</scene>
<scene name='colorSTRUCTURE'>structure</scene>
{{Template:ColorKey Composition Protein}}, {{Template:ColorKey Composition DNA}}

Revision as of 03:58, 13 May 2011

A comparison of the Replication Terminator Protein (from Bacillus subtillis) and Tus (from Escerishia coli) provides an interesting insight into how proteins with vastly different structures and mechanisms of action can produce essentially identical effects in their native systems.

Looking at the structures of these two proteins, it is not immediately obvious that they would perfom the same function, specifically, to arrest the progression of the replication fork along the bacterial chromosome at specific sites (termed Ter sites). Furthermore, this arrest-mechanism functions in a polar manner in both organisms, which is perhaps surprising considering the symmetrical characteristics of both proteins.

Tus complexed with Ter DNA (Kamada

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Protein, DNA

RTP complexed with

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Protein, DNA

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Rada Germanos, Michal Harel, Alexander Berchansky