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

Abstract:

:Initiation of σ(54)-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 σ(54) (σ(54)(RI)) 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.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Zhang N,Joly N,Buck M

doi

10.1093/nar/gks661

subject

Has Abstract

pub_date

2012-10-01 00:00:00

pages

9139-52

issue

18

eissn

0305-1048

issn

1362-4962

pii

gks661

journal_volume

40

pub_type

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