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MucR binds multiple target sites in the promoter of its own gene and is a heat-stable protein: Is MucR a H-NS-like protein?
Baglivo, Ilaria; Pirone, Luciano; Malgieri, Gaetano; Fattorusso, Roberto; Roop Ii, Roy Martin; Pedone, Emilia Maria; Pedone, Paolo Vincenzo.
Afiliação
  • Baglivo I; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies University of Campania 'Luigi Vanvitelli' Caserta Italy.
  • Pirone L; Institute of Biostructures and Bioimaging C.N.R. Naples Italy.
  • Malgieri G; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies University of Campania 'Luigi Vanvitelli' Caserta Italy.
  • Fattorusso R; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies University of Campania 'Luigi Vanvitelli' Caserta Italy.
  • Roop Ii RM; Department of Microbiology and Immunology Brody School of Medicine East Carolina University Greenville NC USA.
  • Pedone EM; Institute of Biostructures and Bioimaging C.N.R. Naples Italy.
  • Pedone PV; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies University of Campania 'Luigi Vanvitelli' Caserta Italy.
FEBS Open Bio ; 8(4): 711-718, 2018 04.
Article em En | MEDLINE | ID: mdl-29632823
ABSTRACT
The protein MucR from Brucella spp. is involved in the expression regulation of genes necessary for host interaction and infection. MucR is a member of the Ros/MucR family, which comprises prokaryotic zinc-finger proteins and includes Ros from Agrobacterium tumefaciens and the Ml proteins from Mesorhizobium loti. MucR from Brucella spp. can regulate the expression of virulence genes and repress its own gene expression. Despite the well-known role played by MucR in the repression of its own gene, no target sequence has yet been identified in the mucR promoter gene. In this study, we provide the first evidence that MucR from Brucella abortus binds more than one target site in the promoter region of its own gene, suggesting a molecular mechanism by which this protein represses its own expression. Furthermore, a circular dichroism analysis reveals that MucR is a heat-stable protein. Overall, the results of this study suggest that MucR might resemble a H-NS protein.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2018 Tipo de documento: Article