ArticleInternational journal of biological sciences2011
The DNA binding and bending activities of truncated tail-less HMGB1 protein are differentially affected by Lys-2 and Lys-81 residues and their acetylation.
Article in International journal of biological sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- HMGB3: A pivotal orchestrator of therapy resistance and cancer stemness in human malignancies (Review).Oncology reports · 2026Review
- The Role of the HMGB1 C-Terminal Domain in Epithelial-Mesenchymal Transition and Invasion in 2D and 3D MDA-MB-231 Breast Cancer Models.International journal of molecular sciences · 2026Article
- Article
- Posttranslational S-nitrosylation modification regulates HMGB1 secretion and promotes its proinflammatory and neurodegenerative effects.Cell reports · 2022Article
- Effect of in vivo post-translational modifications of the HMGB1 protein upon binding to platinated DNA: a molecular simulation study.Nucleic acids research · 2018Article
- Effects of mimicked acetylated HMGB1 on macrophages and dendritic cells.Molecular medicine reports · 2018Article
- High-Mobility Group Box-1 and Liver Disease.Hepatology communications · 2018Review
- Review
- Unconventional Pathways of Secretion Contribute to Inflammation.International journal of molecular sciences · 2017Review
- HMGB1 bound to cisplatin-DNA adducts undergoes extensive acetylation and phosphorylationChemical science · 2015Article
- High-mobility group box 1 is a novel deacetylation target of Sirtuin1.Kidney international · 2015Article
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- Article
- Role of the acidic tail of high mobility group protein B1 (HMGB1) in protein stability and DNA bending.PloS one · 2013Article
- Combinatorial control of gene expression.BioMed research international · 2013Review
- The high mobility group box: the ultimate utility player of a cell.Trends in biochemical sciences · 2012Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The role of lysines 2 and 81 as target sites for acetylation in full-length HMGB1 and truncated tail-less protein, respectively, has been studied by mutation analysis for the abilities of these proteins to bind and bend DNA. The DNA bending ability of truncated tail-less HMGB1 containing Lys-2 mutated to alanine does not differ from that of the wild-type protein, while the same mutation of Lys-81 reduced the bending capacity of the mutant protein. These data demonstrate that Lys-81 is critical for the DNA bending ability of truncated HMGB1. Such a conclusion is further confirmed by the experiments carried out with CBP-acetylated proteins: acetylation of Lys-2 in mutant protein K81/A81 alleviated DNA bending and induced DNA end-joining. On the contrary, the acetylation of Lys-81 in the mutant K2/A2 enhanced the bending potential of HMGB1∆C. Regarding the ability of HMGB1 to specifically bind bent DNA, the individual mutations of either K2 or K81 as well as the double mutation of both residues to alanine were found to completely abolish binding of truncated tail-less HMGB1 to cisplatin-modified DNA. We conclude that unlike the case with the bending ability of truncated HMGB1, where Lys-81 has a primary function, Lys-2 and Lys-81 are both critical for the protein's binding to cisplatin-modified DNA. The mutation K2/A2 in full-length HMGB1 and acidic tail removal induce the same conformational changes. Any further substitutions at the acetylable lysines in the truncated form of HMGB1 do not have an additional effect.
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