T7 RNA Polymerase: Difference between revisions

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'''The growing hybrid induces protein domain movement'''. Also note that the initial active site accommodates only about a 3 base RNA-DNA duplex, as the N-terminal domain lies in the path of that hybrid (remember that forward translocation of the polymerase is really reverse translocation of the RNA-DNA hybrid). Beyond about 3 bases, the hybrid pushes on the N-terminal domain, inducing into to both translate backwards and rotate. This can be seen in structures of the complex with 7 and 8 bases of RNA synthesized.
'''The growing hybrid induces protein domain movement'''. Also note that the initial active site accommodates only about a 3 base RNA-DNA duplex, as the N-terminal domain lies in the path of that hybrid (remember that forward translocation of the polymerase is really reverse translocation of the RNA-DNA hybrid). Beyond about 3 bases, the hybrid pushes on the N-terminal domain, inducing into to both translate backwards and rotate. This can be seen in structures of the complex with 7 and 8 bases of RNA synthesized.


'''Transition to Elongation'''. Toward the end of the above rotation, stress builds up in the promoter binding domain, leading to a weakening of some of the interactions with the upstream duplex promoter. This triggers promoter release, which now allows the N-terminal domain to rotate 220° in the ''other'' direction, to form the <scene name='77/778917/T7rp_elongation_cmplx_full_vw/1'>elongation complex</scene>.
'''Transition to Elongation'''. Toward the end of the above rotation (at about a 9mer RNA), stress builds up in the promoter binding domain, leading to a weakening of some of the interactions with the upstream duplex promoter. This triggers promoter release, which now allows the N-terminal domain to rotate 220° in the ''other'' direction, to form the <scene name='77/778917/T7rp_elongation_cmplx_full_vw/1'>elongation complex</scene>.


== Function ==
== Function ==