DSpace UNL

RUN >
Faculdade de Ciências e Tecnologia (FCT) >
FCT Departamentos >
FCT: Departamento de Ciências da Vida >
FCT: DCV - Artigos em revista internacional com arbitragem científica >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/4204

Title: Probing key DNA contacts in AraR-mediated transcriptional repression of the Bacillus subtilis arabinose regulon.
Authors: Sá-Nogueira, Isabel de
Franco, Irina Saraiva
Mota, Luís Jaime
Soares, Cláudio Manuel
Issue Date: 5-Jul-2007
Publisher: Oxford University Press
Citation: Franco. I.S. Mota. L.J. Soares. C.M. and de Sá-Nogueira I. (2007) Probing key DNA contacts in AraR-mediated transcriptional repression of the Bacillus subtilis arabinose regulon. Nucleic Acids Research 35: 4755–4766.
Abstract: In the absence of arabinose, the AraR transcription factor represses the expression of genes involved in the utilization of arabinose, xylose and galactose in Bacillus subtilis. AraR exhibits a chimeric organization: the N-terminal DNA-binding region belongs to the GntR family and the C-terminal effector-binding domain is homologous to the GalR/LacI family. Here, the AraR-DNA-binding interactions were characterized in vivo and in vitro. The effect of residue substitutions in the AraR N-terminal domain and of base-pair exchanges into an AraR-DNA-binding operator site were examined by assaying for AraR-mediated regulatory activity in vivo and DNA-binding activity in vitro. The results showed that residues K4, R45 and Q61, located in or near the winged-helix DNA-binding motif, were the most critical amino acids required for AraR function. In addition, the analysis of the various mutations in an AraR palindromic operator sequence indicated that bases G9, A11 and T16 are crucial for AraR binding. Moreover, an AraR mutant M34T was isolated that partially suppressed the effect of mutations in the regulatory cis-elements. Together, these findings extend the knowledge on the nature of AraR nucleoprotein complexes and provide insight into the mechanism that underlies the mode of action of AraR and its orthologues.
Description: Nucleic Acid Research (2007) Vol.37 N. 14 4755-4766
URI: http://hdl.handle.net/10362/4204
ISSN: 0305-1048 (Print)
1362-4962 (Online)
Appears in Collections:FCT: DCV - Artigos em revista internacional com arbitragem científica

Files in This Item:

File Description SizeFormat
Franco et al NAR 2007.pdf872.13 kBAdobe PDFView/Open
Statistics
View Statistics
FacebookTwitterDeliciousLinkedInDiggGoogle BookmarksMySpaceOrkut
Formato BibTex mendeley Endnote Logotipo do DeGóis 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Universidade Nova de Lisboa  - Statistics  - Feedback
Estamos no RCAAP Governo Português separator Ministério da Educação e Ciência   Fundação para a Ciência e a Tecnologia

Financiado por:

POS_C UE