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

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

doi:10.1016/j.febslet.2007.02.035

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

FEBS Lett. 2007 Mar 20;581(6):1190-6. doi: 10.1016/j.febslet.2007.02.035. Epub 2007 Feb 28.

Authors

Ekaterina A Rodikova¹, 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

Affiliation

¹ Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Prospekt Nauki 5, Pushchino, Moscow Region 142290, Russia.

PMID: 17346714
DOI: 10.1016/j.febslet.2007.02.035

Abstract

HlyIIR is a negative transcriptional regulator of hemolysin II gene from B. cereus. It binds to a long DNA perfect inverted repeat (44bp) located upstream the hlyII 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacillus cereus / genetics*
Bacterial Proteins / genetics*
Bacterial Toxins / genetics*
Binding Sites
Dimerization
Genes, Bacterial
Hemolysin Proteins / genetics*
Nucleic Acid Conformation
Operator Regions, Genetic*
Protein Binding
Repetitive Sequences, Nucleic Acid*

Substances

ApxII toxin, bacteria
Bacterial Proteins
Bacterial Toxins
Hemolysin Proteins