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Title

Complex interplay between the LysR-type regulator AtzR and its binding site mediates atzDEF activation in response to two distinct signals

AuthorsPorrúa, Odil ; Platero, Ana Isabel ; Santero, Eduardo ; Solar, Gloria del ; Govantes, Fernando
KeywordsBacterial proteins
Base sequence
DNA mutational analysis
Gene expression regulation
Nitrogen
Operon
Triazines
Cyanuric acid
Beta-galactosidase
Pseudomonas putida
Issue Date28-Feb-2010
PublisherJohn Wiley & Sons
CitationMolecular Microbiology 76(2): 331-347 (2010)
AbstractAtzR is a LysR-type regulator responsible for activation of the cyanuric acid utilization operon atzDEF. AtzR binds the PatzDEF promoter region at a strong recognition element, designated the repressor binding site, and a weaker binding determinant, the activator binding site (ABS). AtzR activates transcription in response to two dissimilar signals, nitrogen limitation and cyanuric acid. In the present work we analyse the structure and function of the cis-acting elements involved in AtzR activation of atzDEF. Hydroxyl radical footprinting assays revealed that the ABS is composed of three functional subsites spaced at one helix-turn intervals. Two modes of interaction with the ABS are detected in vitro: AtzR binds at the ABS-2 and ABS-3 subsites in the absence of inducer, and relocates to interact with the ABS-1 and ABS-2 subsites in the presence of cyanuric acid. In vivo mutational analysis indicates that ABS-1 and ABS-2 are required for full PatzDEF activation in all conditions. In contrast, ABS-3 acts as a ‘subunit trap’ that hinders productive AtzR interactions with ABS-1 and ABS-2. Our results strongly suggest an activation model in which cyanuric acid and nitrogen limitation cooperate to reposition AtzR from an inactive, ABS-3 bound configuration to an active, ABS-1- and ABS-2-bound configuration.
Description17 páginas, 7 figuras, 3 tablas.
Publisher version (URL)http://dx.doi.org/10.1111/j.1365-2958.2010.07100.x
URIhttp://hdl.handle.net/10261/41302
DOI10.1111/j.1365-2958.2010.07100.x
ISSN0950-382X
E-ISSN1365-2958
Appears in Collections:(CABD) Artículos
(CIB) Artículos
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