Sankpal, Umesh T. ; Rao, Desirazu N. (2002) Mutational analysis of conserved residues in HhaI DNA methyltransferase Nucliec Acids Research, 30 (12). pp. 2628-2638. ISSN 0305-1048
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Official URL: http://nar.oxfordjournals.org/content/30/12/2628.a...
Related URL: http://dx.doi.org/10.1093/nar/gkf380
Abstract
HhaI DNA methyltransferase belongs to the C5-cytosine methyltransferase family, which is characterized by the presence of a set of highly conserved amino acids and motifs present in an invariant order. HhaI DNA methyltransferase has been subjected to a lot of biochemical and crystallographic studies. A number of issues, especially the role of the conserved amino acids in the methyltransferase activity, have not been addressed. Using sequence comparison and structural data, a structure-guided mutagenesis approach was undertaken, to assess the role of conserved amino acids in catalysis. Site-directed mutagenesis was performed on amino acids involved in cofactor S-adenosyl-L-methionine (AdoMet) binding (Phe18, Trp41, Asp60 and Leu100). Characterization of these mutants, by in vitro /in vivo restriction assays and DNA/AdoMet binding studies, indicated that most of the residues present in the AdoMet-binding pocket were not absolutely essential. This study implies plasticity in the recognition of cofactor by HhaI DNA methyltransferase.
Item Type: | Article |
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Source: | Copyright of this article belongs to Oxford University Press. |
ID Code: | 51204 |
Deposited On: | 28 Jul 2011 07:24 |
Last Modified: | 28 Jul 2011 07:24 |
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