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Diversity of DNA methyltransferases that recognize asymmetric target sequences

Madhusoodanan, UK and Rao, DN (2010) Diversity of DNA methyltransferases that recognize asymmetric target sequences. In: Critical Reviews in biochemistry and molecular biologyBIOLOGY, 45 (2). pp. 125-145.

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Official URL: http://informahealthcare.com/doi/abs/10.3109/10409...

Abstract

DNA methyltransferases (MTases) are a group of enzymes that catalyze the methyl group transfer from S-adenosyl-L-methionine in a sequence-specific manner. Orthodox Type II DNA MTases usually recognize palindromic DNA sequences and add a methyl group to the target base (either adenine or cytosine) on both strands. However, there are a number of MTases that recognize asymmetric target sequences and differ in their subunit organization. In a bacterial cell, after each round of replication, the substrate for any MTase is hemimethylated DNA, and it therefore needs only a single methylation event to restore the fully methylated state. This is in consistent with the fact that most of the DNA MTases studied exist as monomers in solution. Multiple lines of evidence suggest that some DNA MTases function as dimers. Further, functional analysis of many restriction-modification systems showed the presence of more than one or fused MTase genes. It was proposed that presence of two MTases responsible for the recognition and methylation of asymmetric sequences would protect the nascent strands generated during DNA replication from cognate restriction endonuclease. In this review, MTases recognizing asymmetric sequences have been grouped into different subgroups based on their unique properties. Detailed characterization of these unusual MTases would help in better understanding of their specific biological roles and mechanisms of action. The rapid progress made by the genome sequencing of bacteria and archaea may accelerate the identification and study of species- and strain-specific MTases of host-adapted bacteria and their roles in pathogenic mechanisms.</.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Taylor and Francis Group.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 22 Jul 2010 06:31
Last Modified: 22 Jul 2010 06:31
URI: http://eprints.iisc.ernet.in/id/eprint/30940

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