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 Celljournal_title
Molecular cellauthors
Boucher PE,Maris AE,Yang MS,Stibitz Sdoi
10.1016/s1097-2765(03)00007-8subject
Has Abstractpub_date
2003-01-01 00:00:00pages
163-73issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(03)00007-8journal_volume
11pub_type
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