A DEK Domain-Containing Protein Modulates Chromatin Structure and Function in Arabidopsis . Issue 11 (11th November 2014)
- Record Type:
- Journal Article
- Title:
- A DEK Domain-Containing Protein Modulates Chromatin Structure and Function in Arabidopsis . Issue 11 (11th November 2014)
- Main Title:
- A DEK Domain-Containing Protein Modulates Chromatin Structure and Function in Arabidopsis
- Authors:
- Waidmann, Sascha
Kusenda, Branislav
Mayerhofer, Juliane
Mechtler, Karl
Jonak, Claudia - Abstract:
- Abstract : This study identifies DEK3 as a chromatin architectural protein capable of modulating DNA topology, DNA accessibility, and gene expression in Arabidopsis . Furthermore, functional levels of DEK3 are crucial for stress tolerance. Abstract: Chromatin is a major determinant in the regulation of virtually all DNA-dependent processes. Chromatin architectural proteins interact with nucleosomes to modulate chromatin accessibility and higher-order chromatin structure. The evolutionarily conserved DEK domain-containing protein is implicated in important chromatin-related processes in animals, but little is known about its DNA targets and protein interaction partners. In plants, the role of DEK has remained elusive. In this work, we identified DEK3 as a chromatin-associated protein in Arabidopsis thaliana . DEK3 specifically binds histones H3 and H4. Purification of other proteins associated with nuclear DEK3 also established DNA topoisomerase 1α and proteins of the cohesion complex as in vivo interaction partners. Genome-wide mapping of DEK3 binding sites by chromatin immunoprecipitation followed by deep sequencing revealed enrichment of DEK3 at protein-coding genes throughout the genome. Using DEK3 knockout and overexpressor lines, we show that DEK3 affects nucleosome occupancy and chromatin accessibility and modulates the expression of DEK3 target genes. Furthermore, functional levels of DEK3 are crucial for stress tolerance. Overall, data indicate that DEK3 contributesAbstract : This study identifies DEK3 as a chromatin architectural protein capable of modulating DNA topology, DNA accessibility, and gene expression in Arabidopsis . Furthermore, functional levels of DEK3 are crucial for stress tolerance. Abstract: Chromatin is a major determinant in the regulation of virtually all DNA-dependent processes. Chromatin architectural proteins interact with nucleosomes to modulate chromatin accessibility and higher-order chromatin structure. The evolutionarily conserved DEK domain-containing protein is implicated in important chromatin-related processes in animals, but little is known about its DNA targets and protein interaction partners. In plants, the role of DEK has remained elusive. In this work, we identified DEK3 as a chromatin-associated protein in Arabidopsis thaliana . DEK3 specifically binds histones H3 and H4. Purification of other proteins associated with nuclear DEK3 also established DNA topoisomerase 1α and proteins of the cohesion complex as in vivo interaction partners. Genome-wide mapping of DEK3 binding sites by chromatin immunoprecipitation followed by deep sequencing revealed enrichment of DEK3 at protein-coding genes throughout the genome. Using DEK3 knockout and overexpressor lines, we show that DEK3 affects nucleosome occupancy and chromatin accessibility and modulates the expression of DEK3 target genes. Furthermore, functional levels of DEK3 are crucial for stress tolerance. Overall, data indicate that DEK3 contributes to modulation of Arabidopsis chromatin structure and function. … (more)
- Is Part Of:
- The Plant Cell. Volume 26:Issue 11(2014)
- Journal:
- The Plant Cell
- Issue:
- Volume 26:Issue 11(2014)
- Issue Display:
- Volume 26, Issue 11 (2014)
- Year:
- 2014
- Volume:
- 26
- Issue:
- 11
- Issue Sort Value:
- 2014-0026-0011-0000
- Page Start:
- 4328
- Page End:
- 4344
- Publication Date:
- 2014-11-11
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.114.129254 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16348.xml