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Bacterial Enhancer Binding Proteins-AAA+ Proteins in Transcription Activation.


ABSTRACT: Bacterial enhancer-binding proteins (bEBPs) are specialised transcriptional activators. bEBPs are hexameric AAA+ ATPases and use ATPase activities to remodel RNA polymerase (RNAP) complexes that contain the major variant sigma factor, ?54 to convert the initial closed complex to the transcription competent open complex. Earlier crystal structures of AAA+ domains alone have led to proposals of how nucleotide-bound states are sensed and propagated to substrate interactions. Recently, the structure of the AAA+ domain of a bEBP bound to RNAP-?54-promoter DNA was revealed. Together with structures of the closed complex, an intermediate state where DNA is partially loaded into the RNAP cleft and the open promoter complex, a mechanistic understanding of how bEBPs use ATP to activate transcription can now be proposed. This review summarises current structural models and the emerging understanding of how this special class of AAA+ proteins utilises ATPase activities to allow ?54-dependent transcription initiation.

SUBMITTER: Gao F 

PROVIDER: S-EPMC7175178 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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Bacterial Enhancer Binding Proteins-AAA<sup>+</sup> Proteins in Transcription Activation.

Gao Forson F   Danson Amy E AE   Ye Fuzhou F   Jovanovic Milija M   Buck Martin M   Zhang Xiaodong X  

Biomolecules 20200225 3


Bacterial enhancer-binding proteins (bEBPs) are specialised transcriptional activators. bEBPs are hexameric AAA<sup>+</sup> ATPases and use ATPase activities to remodel RNA polymerase (RNAP) complexes that contain the major variant sigma factor, σ<sup>54</sup> to convert the initial closed complex to the transcription competent open complex. Earlier crystal structures of AAA<sup>+</sup> domains alone have led to proposals of how nucleotide-bound states are sensed and propagated to substrate inte  ...[more]

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