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Nucleic Acids Research, Vol 25, Issue 14 2841-2846, Copyright © 1997 by Oxford University Press

ARTICLES

Footprint analysis of the bsp RI DNA methyltransferase-DNA interaction

C Finta and A Kiss
Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, PO Box 521, Szeged 6701, Hungary.

The interaction between the GGCC-specific Bsp RI DNA methyltransferase (M. Bsp RI) and substrate DNA was studied with footprinting techniques using a DNA fragment that was unmodified on both strands. Footprinting with DNase I revealed an approximately 14 bp protected region. Footprinting with dimethylsulfate detected major groove interactions with the guanine bases of the recognition sequence. Reaction with 1,10- phenanthroline-copper did not show protection, suggesting that minor groove interactions play little role in sequence-specific recognition by M. Bsp RI. Hydroxyl radical footprinting revealed a protected stretch of 6 nt. The hydroxyl radical footprint of M. Bsp RI differs markedly from the the footprint reported for the Hha I and Sss I methyltransferases. The pattern of protection from dimethylsulfate and hydroxyl radicals suggests that the interactions of M. Bsp RI with DNA are similar to those detected in the co-crystal structure of the Hae III methyltransferase.
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T. Rasko, C. Finta, and A. Kiss
DNA bending induced by DNA (cytosine-5) methyltransferases
Nucleic Acids Res., August 15, 2000; 28(16): 3083 - 3091.
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