Please use this identifier to cite or link to this item:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Mechanism of antiactivation at the pseudomonas sp. strain ADP σN-dependent PatzT promoter

AuthorsPlatero, Ana Isabel CSIC; López-Sánchez, Aroa CSIC; Tomás-Gallardo, Laura CSIC ORCID; Santero, Eduardo CSIC ORCID; Govantes, Fernando CSIC ORCID
Issue Date2016
PublisherAmerican Society for Microbiology
CitationApplied and Environmental Microbiology 82(14): 4350-4362 (2016)
AbstractPatzT is an internal promoter of the atzRSTUVW operon that directs the synthesis of AtzT, AtzU, AtzV, and AtzW, components of an ABC-type cyanuric acid transport system. PatzT is σ dependent, activated by the general nitrogen control regulator NtrC with the assistance of protein integration host factor (IHF), and repressed by the LysR-type transcriptional regulator (LTTR) AtzR. We have used a variety of in vivo and in vitro gene expression and protein-DNA interaction assays to assess the mechanisms underlying AtzR-dependent repression of PatzT. Here, we show that repression only occurs when AtzR and NtrC interact simultaneously with the PatzT promoter region, indicating that AtzR acts as an antiactivator to antagonize activation by NtrC. Furthermore, repression requires precise rotational orientation of the AtzR and NtrC binding sites, strongly suggesting proteinprotein interaction between the two proteins on the promoter region. Further exploration of the antiactivation mechanism showed that although AtzR-dependent repression occurs prior to open complex formation, AtzR does not alter the oligomerization state of NtrC or inhibit NtrC ATPase activity when bound to the PatzT promoter region. Taken together, these results strongly suggest that PatzT-bound AtzR interacts with NtrC to prevent the coupling of NtrC-mediated ATP hydrolysis with the remodeling of the interactions between E-σ and PatzT that lead to open complex formation.
Identifiersdoi: 10.1128/AEM.00906-16
e-issn: 1098-5336
issn: 0099-2240
Appears in Collections:(CABD) Artículos

Files in This Item:
File Description SizeFormat
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work


checked on Nov 30, 2021


checked on Dec 1, 2021

Google ScholarTM




WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.