ArticleNucleic acids research2009
The yeast high mobility group protein HMO2, a subunit of the chromatin-remodeling complex INO80, binds DNA ends.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Targeting DNA termini with a small-molecule natural product analogue: a DNA end-binder (DEB) to augment DNA double-strand breaks.Nucleic acids research · 2025Article
- Autoinhibition imposed by a large conformational switch of INO80 regulates nucleosome positioning.Science (New York, N.Y.) · 2025Article
- Article
- Yeast HMO1: Linker Histone Reinvented.Microbiology and molecular biology reviews : MMBR · 2017Review
- The N-terminal Region of Chromodomain Helicase DNA-binding Protein 4 (CHD4) Is Essential for Activity and Contains a High Mobility Group (HMG) Box-like-domain That Can Bind Poly(ADP-ribose).The Journal of biological chemistry · 2016Article
- Yeast high mobility group protein HMO1 stabilizes chromatin and is evicted during repair of DNA double strand breaks.Nucleic acids research · 2015Article
- Cloning, purification, crystallization and preliminary X-ray studies of HMO2 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2014Article
- C-terminal low-complexity sequence repeats of Mycobacterium smegmatis Ku modulate DNA binding.Bioscience reports · 2013Article
- A network of HMG-box transcription factors regulates sexual cycle in the fungus Podospora anserina.PLoS genetics · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA damage is a common hazard that all cells have to combat. Saccharomyces cerevisiae HMO2 is a high mobility group protein (HMGB) that is a component of the chromatin-remodeling complex INO80, which is involved in double strand break (DSB) repair. We show here using DNA end-joining and exonuclease protection assays that HMO2 binds preferentially to DNA ends. While HMO2 binds DNA with both blunt and cohesive ends, the sequence of a single stranded overhang significantly affects binding, supporting the conclusion that HMO2 recognizes features at DNA ends. Analysis of the effect of duplex length on the ability of HMO2 to protect DNA from exonucleolytic cleavage suggests that more than one HMO2 must assemble at each DNA end. HMO2 binds supercoiled DNA with higher affinity than linear DNA and has a preference for DNA with lesions such as pairs of tandem mismatches; however, comparison of DNA constructs of increasing length suggests that HMO2 may not bind stably as a monomer to distorted DNA. The remarkable ability of HMO2 to protect DNA from exonucleolytic cleavage, combined with reports that HMO2 arrives early at DNA DSBs, suggests that HMO2 may play a role in DSB repair beyond INO80 recruitment.
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