ArticleFEBS open bio2013
Nucleosome structural changes induced by binding of non-histone chromosomal proteins HMGN1 and HMGN2.
Article in FEBS open bio, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications.RSC chemical biology · 2021Article
- Exogenous HMGN2 inhibits the migration and invasion of osteosarcoma cell lines.Translational cancer research · 2020Article
- Optimized Cross-Linking Mass Spectrometry for in Situ Interaction Proteomics.Journal of proteome research · 2019Article
- Effect of HMGN2 on proliferation and apoptosis of MCF-7 breast cancer cells.Oncology letters · 2019Article
- Spermatid-specific linker histone HILS1 is a poor condenser of DNA and chromatin and preferentially associates with LINE-1 elements.Epigenetics & chromatin · 2018Article
- Increased expression of high-mobility group nucleosomal-binding domain 2 protein in various tumor cell lines.Oncology letters · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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Abstract
Interactions between the nucleosome and the non-histone chromosomal proteins (HMGN1 and HMGN2) were studied by circular dichroism (CD) spectroscopy to elucidate structural changes in the nucleosome induced by HMGN binding. Unlike previous studies that used a nucleosome extracted from living cells, in this study we utilized a nucleosome reconstituted from unmodified recombinant histones synthesized in Escherichia coli and a 189-bp synthetic DNA fragment harboring a nucleosome positioning sequence. This DNA fragment consists of 5'-TATAAACGCC-3' repeats that has a high affinity to the histone octamer. A nucleosome containing a unique octamer-binding sequence at a specific location on the DNA was produced at sufficiently high yield for spectroscopic analysis. CD data have indicated that both HMGN1 and HMGN2 can increase the winding angle of the nucleosome DNA, but the extent of the structural changes induced by these proteins differs significantly. This suggests HMGN1 and HMGN2 would have different abilities to facilitate nucleosome remodeling.
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Registered trials
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