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CryoEM of Mycobacterium tuberculosis WT RNAP holoenzyme/RbpA bound to an inhibitor corallopyronin and us-fork DNA


ABSTRACT:

SUBMITTER: Elizabeth A Campbell 

PROVIDER: EMPIAR-10897 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

Structures of an RNA polymerase promoter melting intermediate elucidate DNA unwinding.

Boyaci Hande H   Chen James J   Jansen Rolf R   Darst Seth A SA   Campbell Elizabeth A EA  

Nature 20190109 7739


A key regulated step of transcription is promoter melting by RNA polymerase (RNAP) to form the open promoter complex<sup>1-3</sup>. To generate the open complex, the conserved catalytic core of the RNAP combines with initiation factors to locate promoter DNA, unwind 12-14 base pairs of the DNA duplex and load the template-strand DNA into the RNAP active site. Formation of the open complex is a multi-step process during which transient intermediates of unknown structure are formed<sup>4-6</sup>.  ...[more]

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