Meeting Agenda:
 

Scientific work presentation:

Speaker: Jobichen Chacko

Talk title:     Structural and functional studies of DNMT1 to understand its role in DNA methylation

Abstract

DNA methylation is an epigenetic mechanism implicated in transcriptional regulation, genomic imprinting and silencing of repetitive DNA elements. The addition of methyl groups is controlled at several different levels in cells and is carried out by a family of enzymes called DNA methyltransferases (DNMTs). DNMT1 mediates the maintenance of established patterns of DNA methylation. DNMT1 is a multimodular protein composed of a replication foci-targeting domain (RFD), a DNA-binding CXXC domain, a pair of bromo-adjacent homology (BAH) domains and a C-terminal catalytic domain. The structure of DNMT1-DNA complex is already reported and it reveals the binding regions of DNMT1 with DNA. Recent studies have shown that various RNA fragments also bind to DNMT1 to prevent genomic methylation. The pull-down assay using the various domains of DNMT1 showed that the C-terminal region is involved in binding to RNA. We have expressed and purified various fragments from human-DNMT1 in order to gain further insights by elucidating the structure of DNMT1-RNA complex.