The response regulator BvgA and RNA polymerase alpha subunit C-terminal domain bind simultaneously to different faces of the same segment of promoter DNA.

Abstract:

:Examination of the binding of FeBABE-conjugated BvgA to the fha promoter of Bordetella pertussis has revealed that three dimers, formed by head-to-head association of monomers, bind one face of the DNA helix from the inverted-heptad primary binding site to the -35 region. The orientation of BvgA monomers within the dimers is the same as that recently demonstrated by X-ray crystallographic methods for a dimer of the C-terminal domain of NarL bound to DNA. Use of FeBABE conjugates of RNAP alpha subunit C-terminal domain showed that binding of this domain is linearly coincident with binding of the BvgA dimers, but to a different helical face. These results reveal a previously undescribed mode of interaction between RNAP alpha-CTD and a transcriptional activator.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Boucher PE,Maris AE,Yang MS,Stibitz S

doi

10.1016/s1097-2765(03)00007-8

subject

Has Abstract

pub_date

2003-01-01 00:00:00

pages

163-73

issue

1

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(03)00007-8

journal_volume

11

pub_type

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