Recombinant Histone H1 Catalog No: 81126, 81826 Quantity: 100, 1000 Μg Expressed In: E

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Recombinant Histone H1 Catalog No: 81126, 81826 Quantity: 100, 1000 Μg Expressed In: E

Recombinant Histone H1 Catalog No: 81126, 81826 Quantity: 100, 1000 µg Expressed In: E. coli Concentration: 0.4 µg/µl Source: Human Buffer Contents: Recombinant Histone H1 in 25 mM Tris-HCl pH 8.0, 300 mM NaCl, 10% glycerol. Background: Histone H1, also called as H1F0 (H1 Histone Family Member 0), is a replacement subtype, and replicationindependent histone, which is a member of the histone H1 family. It involves in basal repression of gene expression. H1 can act as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation. Diseases associated with H1F0 include Retinal Cancer and Deafness, Autosomal Dominant. Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker- histone H1, with the DNA between the nucleosomes to form higher order chromatin structures. Histone H1present at the interface between the nucleosome core and DNA entry/exit points. Protein Details: Full length Histone H1 (accession number NP_005309.1) was expressed in E. coli cells with no tag. The molecular weight of Histone H1 is 21 kDa. Recombinant Histone H1 protein gel Application Notes: Recombinant Histone H1 is suitable for use as substrates in the 12.5% SDS-PAGE Coomassie staining study of enzyme kinetics, inhibitor screening, and selectivity profiling. Purity: >85% Storage and Guarantee: Recombinant proteins in solution are temperature sensitive and must be stored at -80°C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage. This product is for research use only and is not for use in diagnostic procedures. This product is guaranteed for 6 months from date of arrival. North America 877 222 9543 • Europe +32 (0)2 653 0001 • Japan +81 (0)3 5225 3638 • www.activemotif.com.

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How Human H1 Histone Recognizes DNA
molecules Article How Human H1 Histone Recognizes DNA Olesya P. Luzhetskaya, Sergey E. Sedykh and Georgy A. Nevinsky * Institute of Chemical Biology and Fundamental Medicine, SD of Russian Academy of Sciences, 8 Lavrentiev Ave., 630090 Novosibirsk, Russia; [email protected] (O.P.L.); [email protected] (S.E.S.) * Correspondence: [email protected]; Tel.: +7-383-363-51-26; Fax: +7-383-363-51-53 Received: 11 August 2020; Accepted: 1 October 2020; Published: 5 October 2020 Abstract: 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 = 1–20) was evaluated using their competition with 12-mer [32P]labeled oligonucleotide and protein–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) 2 ± 10 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 = 2–6 (which are covered by this protein globule) is approximately 0.33 0.02 M.
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Supplemental Data.Pdf
Supplementary material -Table of content Supplementary Figures (Fig 1- Fig 6) Supplementary Tables (1-13) Lists of genes belonging to distinct biological processes identified by GREAT analyses to be significantly enriched with UBTF1/2-bound genes Supplementary Table 14 List of the common UBTF1/2 bound genes within +/- 2kb of their TSSs in NIH3T3 and HMECs. Supplementary Table 15 List of gene identified by microarray expression analysis to be differentially regulated following UBTF1/2 knockdown by siRNA Supplementary Table 16 List of UBTF1/2 binding regions overlapping with histone genes in NIH3T3 cells Supplementary Table 17 List of UBTF1/2 binding regions overlapping with histone genes in HMEC Supplementary Table 18 Sequences of short interfering RNA oligonucleotides Supplementary Table 19 qPCR primer sequences for qChIP experiments Supplementary Table 20 qPCR primer sequences for reverse transcription-qPCR Supplementary Table 21 Sequences of primers used in CHART-PCR Supplementary Methods Supplementary Fig 1. (A) ChIP-seq analysis of UBTF1/2 and Pol I (POLR1A) binding across mouse rDNA. UBTF1/2 is enriched at the enhancer and promoter regions and along the entire transcribed portions of rDNA with little if any enrichment in the intergenic spacer (IGS), which separates the rDNA repeats. This enrichment coincides with the distribution of the largest subunit of Pol I (POLR1A) across the rDNA. All sequencing reads were mapped to the published complete sequence of the mouse rDNA repeat (Gene bank accession number: BK000964). The graph represents the frequency of ribosomal sequences enriched in UBTF1/2 and Pol I-ChIPed DNA expressed as fold change over those of input genomic DNA.
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