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Two HlyIIR dimers bind to a long perfect inverted repeat in the operator of the hemolysin II gene from Bacillus cereus

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Published copy (DOI)

Author(s)

  • Ekaterina A. Rodikova
  • Oleg V. Kovalevskiy
  • Sergey G. Mayorov
  • Zhanna I. Budarina
  • Victor V. Marchenkov
  • Bogdan S. Melnik
  • Andrew P. Leech
  • Dmitri V. Nikitin
  • Michael G. Shlyapnikov
  • Alexander S. Solonin

Department/unit(s)

Publication details

JournalFEBS Letters
DatePublished - 20 Mar 2007
Issue number6
Volume581
Number of pages7
Pages (from-to)1190-1196
Original languageEnglish

Abstract

HlyIIR is a negative transcriptional regulator of hemolysin II gene from B. cereus. It binds to a long DNA perfect inverted repeat (44 bp) located upstream the hlyll gene. Here we show that HlyIIR is dimeric in solution and in bacterial cells. No protein-protein interactions between dimers and no significant modification of target DNA conformation upon complex formation were observed. Two HlyIIR dimers were found to bind to native operator independently with Kd level in the nanomolar range. The minimal HlyIIR binding site was identified as a half of the long DNA perfect inverted repeat. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

    Research areas

  • TetR family, DNA-binding, transcriptional regulator, CONFORMATIONAL-CHANGES, PROTEIN-DNA, THURINGIENSIS, REPRESSOR, SEQUENCE, ANTHRACIS, FAMILY, TOXINS, ASSAY

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