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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
Author(s) -
Rodikova Ekaterina A.,
Kovalevskiy Oleg V.,
Mayorov Sergey G.,
Budarina Zhanna I.,
Marchenkov Victor V.,
Melnik Bogdan S.,
Leech Andrew P.,
Nikitin Dmitri V.,
Shlyapnikov Michael G.,
Solonin Alexander S.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.02.035
Subject(s) - dna , hemolysin , inverted repeat , bacillus cereus , gene , microbiology and biotechnology , operator (biology) , biology , chemistry , genetics , stereochemistry , gene expression , bacteria , repressor , genome , virulence
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 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.