Insulator function and topological domain border strength scale with architectural protein occupancy

• Type of Material: Article
• Authors: Kevin Van Bortle, Emory University; Michael H Nichols, Emory University; Li Li, Emory University; Ong Chin-Tong, Emory University; Naomi Takenaka, Emory University; Zhaohui Qin, Emory University; Victor Corces, Emory University
• Language: English
• Date: 2014-01-01
• Publisher: BioMed Central
• Publication Version: Final Published Version
• Copyright Statement: © 2014 Van Bortle et al.; licensee BioMed Central Ltd.
• License: Creative Commons Attribution 4.0 International
• Final Published Version (URL): http://genomebiology.com/2014/15/6/R82
• Title of Journal or Parent Work: Genome Biology
• ISSN: 1465-6906
• Volume: 15
• Issue: 6
• Start Page: R82
• End Page: R82
• Grant/Funding Information: This work was supported by US Public Health Service Award R01GM035463 from the National Institutes of Health.; The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.; We thank the Drosophila Genomic Resource Center (supported by NIH grant OD010949-10) for reagents, and The Genomic Services Lab at the HudsonAlpha Institute for Biotechnology for their help in performing Illumina sequencing of ChIP-Seq samples.
• Keywords: Science & Technology; Genetics & Heredity; RNA-POLYMERASE III; ORGANIZATION; COHESIN; INTEGRATIVE GENOMICS VIEWER; BINDING FACTOR; DROSOPHILA GENOME; CHROMATIN INTERACTIONS; EMBRYONIC STEM-CELLS; Biotechnology & Applied Microbiology; GENE-EXPRESSION; TRANSCRIPTION; Life Sciences & Biomedicine
• Research Categories: Biology, Bioinformatics; Biology, Biostatistics

Abstract

Chromosome conformation capture studies suggest that eukaryotic genomes are organized into structures called topologically associating domains. The borders of these domains are highly enriched for architectural proteins with characterized roles in insulator function. However, a majority of architectural protein binding sites localize within topological domains, suggesting sites associated with domain borders represent a functionally different subclass of these regulatory elements. How topologically associating domains are established and what differentiates border-associated from non-border architectural protein binding sites remain unanswered questions.