DNA recognition by the EcoP15I and EcoPI modification methyltransferases

Ahmad, Ishtiyaque ; Krishnamurthy, Vinita ; Rao, Desirazu N. (1995) DNA recognition by the EcoP15I and EcoPI modification methyltransferases Gene, 157 (1-2). pp. 143-147. ISSN 0378-1119

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/037811...

Related URL: http://dx.doi.org/10.1016/0378-1119(95)00671-R


The DNA-binding properties of the EcoP15I DNA methyltransferase (M·EcoP15I; MTase) were studied using electro-phoretic mobility shift assays. We show by molecular size-exclusion chromatography and dimethyl suberimidate cross-linking that M·EcoP15I is a dimer in solution. While M·EcoP15I binds approx, threefold more tightly to its recognition sequence, 5'-CAGCAG-3', than to non-specific sequences in the presence of AdoMet or its analogs, the discrimination between specific and non-specific sequences significantly increases in presence of ATP. These results suggest for the first time a role for ATP in DNA recognition by type-III restriction-modification enzymes. Furthermore, we show that although c2, EcoPI mutant MTases are defective in AdoMet binding, they are still able to bind DNA in a sequence-specific manner.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:DNA Binding; Restriction-modification; Protein-DNA Interaction
ID Code:51209
Deposited On:28 Jul 2011 07:23
Last Modified:28 Jul 2011 07:23

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