How Human H1 Histone Recognizes DNA
| العنوان: | How Human H1 Histone Recognizes DNA |
|---|---|
| المؤلفون: | Georgy A. Nevinsky, Sergey E. Sedykh, Olesya P. Luzhetskaya |
| المصدر: | Molecules Volume 25 Issue 19 Molecules, Vol 25, Iss 4556, p 4556 (2020) |
| بيانات النشر: | Multidisciplinary Digital Publishing Institute, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | animal structures, Stereochemistry, DNA, Single-Stranded, Pharmaceutical Science, 010402 general chemistry, 01 natural sciences, Article, Analytical Chemistry, Histones, lcsh:QD241-441, 03 medical and health sciences, chemistry.chemical_compound, lcsh:Organic chemistry, Histone H1, Drug Discovery, Humans, Nucleotide, Physical and Theoretical Chemistry, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, oligonucleotides, biology, Oligonucleotide, Ligand, Organic Chemistry, patterns of DNA recognition, 0104 chemical sciences, Chromatin, human H1 histone, Histone, chemistry, Chemistry (miscellaneous), embryonic structures, biology.protein, Molecular Medicine, Linker, DNA |
| الوصف: | Linker H1 histone is one of the five main histone proteins (H1, H2A, H2B, H3, and H4), which are components of chromatin in eukaryotic cells. Here we have analyzed the patterns of DNA recognition by free H1 histone using a stepwise increase of the ligand complexity method the affinity of H1 histone for various single- and double-stranded oligonucleotides (d(pN)n n = 1&ndash 20) was evaluated using their competition with 12-mer [32P]labeled oligonucleotide and protein&ndash oligonucleotide complex delaying on nitrocellulose membrane filters. It was shown that minimal ligands of H1 histone (like other DNA-dependent proteins and enzymes) are different mononucleotides (dNMPs Kd = (1.30 ± 0.2) × 10&minus 2 M). An increase in the length of single-stranded (ss) homo- and hetero-oligonucleotides (d(pA)n, d(pT)n, d(pC)n, and d(pN)n with different bases) by one nucleotide link regardless of their bases, leads to a monotonic increase in their affinity by a factor of f = 3.0 ± 0.2. This factor f corresponds to the Kd value = 1/f characterizing the affinity of one nucleotide of different ss d(pN)n for H1 at n = 2&ndash 6 (which are covered by this protein globule) is approximately 0.33 ± 0.02 M. The affinity of five out of six DNA nucleotide units is approximately 25 times lower than for one of the links. The affinity of duplexes of complementary homo- and hetero-d(pN)20 is only 1.3&ndash 3.3-fold higher in comparison with corresponding ss oligonucleotides. H1 histone forms mainly weak additive contacts with internucleoside phosphate groups of ssDNAs and one chain of double-stranded DNAs, but not with the bases. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 1420-3049 |
| DOI: | 10.3390/molecules25194556 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::347668988469b9f91567d1187608a035 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....347668988469b9f91567d1187608a035 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14203049 |
|---|---|
| DOI: | 10.3390/molecules25194556 |