Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex
Open Access
- 1 October 1999
- journal article
- research article
- Published byĀ Springer NatureĀ inĀ The EMBO Journal
- Vol.Ā 18 Ā (19) , 5175-5186
- https://doi.org/10.1093/emboj/18.19.5175
Abstract
Inducible expression of the aliphatic amidase operon in Pseudomonas aeruginosa is controlled by an antitermination mechanism which allows production of the fullālength transcript only in the presence of smallāmolecule inducers, such as acetamide. Ligandāregulated antitermination is provided by AmiC, the ligandāsensitive negative regulator, and AmiR, the RNAābinding positive regulator. Under nonāinducing or repressing growth conditions, AmiC and AmiR form a complex in which the activity of AmiR is silenced. The crystal structure of the AmiCāAmiR complex identifies AmiR as a new and highly unusual member of the responseāregulator family of bacterial signal transduction proteins, regulated by sequestration rather than phosphorylation. Comparison with the structure of free AmiC reveals the subtle mechanism of ligandāinduced release of AmiR.Keywords
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