| Literature DB >> 22817886 |
Vladimir Svetlov1, Evgeny Nudler.
Abstract
Transcription antiterminator RfaH alternates between closed (inactive) and open (activated) conformation. In this issue of Cell, Burmann et al. show that opening is accompanied by dramatic all-α to all-β refolding of its C-terminal domain. Each of the folds has a distinct function: all-α-fold acts as a specificity determinant, directing RfaH to a small subset of operons, whereas the all-β-fold recruits ribosome, thereby coupling RfaH-stimulated transcription to translation.Entities:
Year: 2012 PMID: 22817886 PMCID: PMC3874879 DOI: 10.1016/j.cell.2012.06.025
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582