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- W1489784069 abstract "A large variety of proteins bind to specific parts of the genome to regulate gene expression, DNA replication, and chromatin structure. DamID is a powerful method used to map the genomic interaction sites of these proteins in vivo. It is based on fusing a protein of interest to E. coli DNA adenine methyltransferase (dam). Expression of this fusion protein in vivo leads to preferential methylation of adenines in DNA surrounding the native binding sites of the dam fusion partner. Because adenine methylation does not occur endogenously in most eukaryotes, it provides a unique tag to mark protein interaction sites. The adenine-methylated DNA fragments are isolated by selective PCR amplification and can be identified by microarray hybridization. We and others have successfully applied DamID to the genome-wide identification of interaction sites of several transcription factors and other chromatin-associated proteins. Here the DamID technology is discussed in detail, and a step-by-step experimental protocol is provided for use in Drosophila cell lines." @default.
- W1489784069 created "2016-06-24" @default.
- W1489784069 creator A5058453365 @default.
- W1489784069 date "2006-01-01" @default.
- W1489784069 modified "2023-09-23" @default.
- W1489784069 title "Heterochromatin composition and function in Drosophila" @default.
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