Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10822692 | Current Opinion in Structural Biology | 2007 | 7 Pages |
Abstract
Bacterial transcription relies on the binding of dissociable sigma (Ï) factors to RNA polymerase (RNAP) for promoter specificity. The major variant sigma factor (Ï54) forms a stable closed complex with RNAP bound to DNA that rarely spontaneously isomerises to an open complex. ATP hydrolysis by bacterial enhancer-binding proteins is used to remodel the RNAP-Ï54-DNA closed complex. Recently, a wealth of structural information on bacterial enhancer-binding proteins has enabled unprecedented insights into their mechanism. These data provide a structural basis for nucleotide binding and hydrolysis, oligomerisation and the conversion of ATPase activity into remodelling events within the RNAP-Ï54 closed complex, and represent advances towards a complete understanding of the Ï54-dependent transcription activation mechanism.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Mathieu Rappas, Daniel Bose, Xiaodong Zhang,