Nucleic Acids Research, Vol 25, Issue 11 2114-2120, Copyright © 1997 by Oxford University Press
A Karyagina, I Shilov, V Tashlitskii, M Khodoun, S Vasil'ev, PCK Lau and I Nikolskaya
The regulation of the Sso II restriction-modification system from Shigella
sonnei was studied in vivo and in vitro . In lacZ fusion experiments, Sso
II methyltransferase (M. Sso II) was found to repress its own synthesis but
stimulate expression of the cognate restriction endonuclease (ENase). The
N-terminal 72 amino acids of M. Sso II, predicted to form a
helix-turn-helix (HTH) motif, was found to be responsible for the specific
DNA-binding and regulatory function of M. Sso II. Similar HTH motifs are
predicted in the N-terminus of a number of 5-methylcytosine
methyltransferases, particularly M. Eco RII, M.dcm and M. Msp I, of which
the ability to regulate autogenously has been proposed. In vitro, the
binding of M. Sso II to its target DNA was investigated using a mobility
shift assay. M. Sso II forms a specific and stable complex with a 140 bp
DNA fragment containing the promoter region of Sso II R-M system. The
dissociation constant (Kd) was determined to be 1.5x10(-8) M. DNaseI
footprinting experiments demonstrated that M. Sso II protects a 48-52 bp
region immediately upstream of the M. Sso II coding sequence which includes
the predicted - 10 promoter sequence of M. Sso II and the -10 and -35
sequences of R. Sso II.
ARTICLES
Specific binding of sso II DNA methyltransferase to its promoter region provides the regulation of sso II restriction-modification gene expression
Institute of BioMedical Chemistry, 10 Pogodinskaya st., Moscow 119832, Russia. ann@agrobio.msk.su
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