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The Linker Histone GH1-HMGA1 Is Involved in Telomere Stability and DNA Damage Repair
- Source :
- Plant Physiology, Plant Physiology, 2018, 177 (1), pp.311-327. ⟨10.1104/pp.17.01789⟩, Plant Physiology, American Society of Plant Biologists, 2018, 177 (1), pp.311-327. ⟨10.1104/pp.17.01789⟩
- Publication Year :
- 2017
-
Abstract
- International audience; Despite intensive searches, few proteins involved in telomere homeostasis have been identified in plants. Here, we used pull-down assays to identify potential telomeric interactors in the model plant species Arabidopsis (Arabidopsis thaliana). We identified the candidate protein GH1-HMGA1 (also known as HON4), an uncharacterized linker histone protein of the High Mobility Group Protein A (HMGA) family in plants. HMGAs are architectural transcription factors and have been suggested to function in DNA damage repair, but their precise biological roles remain unclear. Here, we show that GH1-HMGA1 is required for efficient DNA damage repair and telomere integrity in Arabidopsis. GH1-HMGA1 mutants exhibit developmental and growth defects, accompanied by ploidy defects, increased telomere dysfunction-induced foci, mitotic anaphase bridges, and degraded telomeres. Furthermore, mutants have a higher sensitivity to genotoxic agents such as mitomycin C and γ-irradiation. Our work also suggests that GH1-HMGA1 is involved directly in the repair process by allowing the completion of homologous recombination.
- Subjects :
- 0301 basic medicine
DNA, Bacterial
DNA Repair
Physiology
Telomere-Binding Proteins
Arabidopsis
[SDV.GEN] Life Sciences [q-bio]/Genetics
Plant Science
Fluorescence
Histones
03 medical and health sciences
Telomere Homeostasis
Genetics
Arabidopsis thaliana
Homologous Recombination
Telomerase
HMGA Proteins
[SDV.GEN]Life Sciences [q-bio]/Genetics
biology
Arabidopsis Proteins
HMGA
Articles
Telomere
biology.organism_classification
Chromatin
Cell biology
030104 developmental biology
High-mobility group
Histone
Mutation
biology.protein
Homologous recombination
DNA Damage
Protein Binding
Subjects
Details
- ISSN :
- 15322548 and 00320889
- Volume :
- 177
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Plant physiology
- Accession number :
- edsair.doi.dedup.....00855541d633d834d4254ce081104db0