A common feature from different subunits of a homomeric AAA+ protein contacts three spatially distinct transcription elements

Nan Zhang, Nicolas Joly, Martin Buck

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Initiation of σ54-dependent transcription requires assistance to melt DNA at the promoter site but is impeded by numerous protein-protein and nucleo-protein interactions. To alleviate these inhibitory interactions, hexameric bacterial enhancer binding proteins (bEBP), a subset of the ATPases associated with various cellular activities (AAA+) protein family, are required to remodel the transcription complex using energy derived from ATP hydrolysis. However, neither the process of energy conversion nor the internal architecture of the closed promoter complex is well understood. Escherichia coli Phage shock protein F (PspF), a well-studied bEBP, contains a surface-exposed loop 1 (L1). L1 is key to the energy coupling process by interacting with Region I of σ5454RI) in a nucleotide dependent manner. Our analyses uncover new levels of complexity in the engagement of a multimeric bEBP with a basal transcription complex via several L1s. The mechanistic implications for these multivalent L1 interactions are elaborated in the light of available structures for the bEBP and its target complexes.

Original languageEnglish (US)
Pages (from-to)9139-9152
Number of pages14
JournalNucleic Acids Research
Volume40
Issue number18
DOIs
StatePublished - Oct 2012

ASJC Scopus subject areas

  • Genetics

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