scholarly journals Tandem Histone-Binding Domains Enhance the Activity of a Synthetic Chromatin Effector

2018 ◽  
Vol 7 (3) ◽  
pp. 842-852 ◽  
Author(s):  
Stefan J. Tekel ◽  
Daniel A. Vargas ◽  
Lusheng Song ◽  
Joshua LaBaer ◽  
Michael R. Caplan ◽  
...  
Keyword(s):  
Histone Binding ◽  
Binding Domains

Molecular investigation of the TTD and PHD histone binding domains of the epigenetic regulator UHRF2 .

2021 ◽  
Author(s):  
Shane M. Ginnard ◽  
Alyssa E. Winkler ◽  
Carlos Mellado Fritz ◽  
Tatum Bluhm ◽  
Ray Kemmer ◽  
...  
Keyword(s):  
Histone Binding ◽  
Binding Domains ◽  
Epigenetic Regulator ◽  
Molecular Investigation

scholarly journals Sir3-Nucleosome Interactions in Spreading of Silent Chromatin in Saccharomyces cerevisiae

2008 ◽  
Vol 28 (22) ◽  
pp. 6903-6918 ◽  
Author(s):  
Johannes R. Buchberger ◽  
Megumi Onishi ◽  
Geng Li ◽  
Jan Seebacher ◽  
Adam D. Rudner ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Activity ◽  
Chromatin Fiber ◽  
Silent Chromatin ◽  
Histone H4 ◽  
Histone Binding ◽  
Aaa Atpase ◽  
Binding Domains ◽  
Sir Complex

ABSTRACT Silent chromatin in Saccharomyces cerevisiae is established in a stepwise process involving the SIR complex, comprised of the histone deacetylase Sir2 and the structural components Sir3 and Sir4. The Sir3 protein, which is the primary histone-binding component of the SIR complex, forms oligomers in vitro and has been proposed to mediate the spreading of the SIR complex along the chromatin fiber. In order to analyze the role of Sir3 in the spreading of the SIR complex, we performed a targeted genetic screen for alleles of SIR3 that dominantly disrupt silencing. Most mutations mapped to a single surface in the conserved N-terminal BAH domain, while one, L738P, localized to the AAA ATPase-like domain within the C-terminal half of Sir3. The BAH point mutants, but not the L738P mutant, disrupted the interaction between Sir3 and nucleosomes. In contrast, Sir3-L738P bound the N-terminal tail of histone H4 more strongly than wild-type Sir3, indicating that misregulation of the Sir3 C-terminal histone-binding activity also disrupted spreading. Our results underscore the importance of proper interactions between Sir3 and the nucleosome in silent chromatin assembly. We propose a model for the spreading of the SIR complex along the chromatin fiber through the two distinct histone-binding domains in Sir3.

scholarly journals Histone-Binding Domains in a Human Nuclear Autoantigenic Sperm Protein1

1996 ◽  
Vol 54 (6) ◽  
pp. 1238-1244 ◽  
Author(s):  
Iglika Batova ◽  
G. O′Rand
Keyword(s):  
Histone Binding ◽  
Binding Domains

Identification of the core-histone-binding domains of HMG1 and HMG2

1986 ◽  
Vol 866 (4) ◽  
pp. 242-251 ◽  
Author(s):  
Jordi Bernués ◽  
Enric Espel ◽  
Enrique Querol
Keyword(s):  
Core Histone ◽  
Histone Binding ◽  
The Core ◽  
Binding Domains

scholarly journals Quality of histone modification antibodies undermines chromatin biology research

F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 1160 ◽  
Author(s):  
Goran Kungulovski ◽  
Albert Jeltsch
Keyword(s):  
Polyclonal Antibodies ◽  
Recombinant Antibodies ◽  
Variable Properties ◽  
Post Translational Modification ◽  
Histone Binding ◽  
Binding Domains ◽  
Quality Checks ◽  
Chromatin Biology ◽  
Biology Research

Histone post-translational modification (PTM) antibodies are essential research reagents in chromatin biology. However, they suffer from variable properties and insufficient documentation of quality. Antibody manufacturers and vendors should provide detailed lot-specific documentation of quality, rendering further quality checks by end-customers unnecessary. A shift from polyclonal antibodies towards sustainable reagents like monoclonal or recombinant antibodies or histone binding domains would help to improve the reproducibility of experimental work in this field.

scholarly journals Tandem histone-binding domains enhance the activity of a synthetic chromatin effector

2017 ◽  
Author(s):  
Stefan J. Tekel ◽  
Daniel Vargas ◽  
Lusheng Song ◽  
Joshua LaBaer ◽  
Karmella A. Haynes
Keyword(s):  
Dna Sequences ◽  
Gene Activation ◽  
Transcriptional Regulators ◽  
Binding Activity ◽  
Hek293 Cells ◽  
Histone Binding ◽  
Cell State ◽  
Protein Protein Interaction ◽  
Binding Domains

ABSTRACTFusion proteins that specifically interact with biochemical marks on chromosomes represent a new class of synthetic transcriptional regulators that decode cell state information rather than DNA sequences. In multicellular organisms, information relevant to cell state, tissue identity, and oncogenesis is often encoded as biochemical modifications of histones, which are bound to DNA in eukaryotic nuclei and regulate gene expression states. We have previously reported the development and validation of the “Polycomb-based transcription factor” (PcTF), a fusion protein that recognizes histone modifications through a protein-protein interaction between its polycomb chromodomain (PCD) motif and trimethylated lysine 27 of histone H3 (H3K27me3) at genomic sites. We demonstrated that PcTF activates genes at methyl-histone-enriched loci in cancer-derived cell lines. However, PcTF induces modest activation of a methyl-histone associated reporter compared to a DNA-binding activator. Therefore, we modified PcTF to enhance its target affinity. Here, we demonstrate the activity of a modified regulator called Pc2TF, which has two tandem copies of the H3K27me3-binding PCD at the N-terminus. Pc2TF shows higher affinity for H3K27me3 in vitro and shows enhanced gene activation in HEK293 cells compared to PcTF. These results provide compelling evidence that the intrinsic histone-binding activity of the PCD motif can be used to tune the activity of synthetic histone-binding transcriptional regulators.

scholarly journals Quality of histone modification antibodies undermines chromatin biology research

F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 1160 ◽  
Author(s):  
Goran Kungulovski ◽  
Albert Jeltsch
Keyword(s):  
Polyclonal Antibodies ◽  
Recombinant Antibodies ◽  
Variable Properties ◽  
Post Translational Modification ◽  
Histone Binding ◽  
Binding Domains ◽  
Quality Checks ◽  
Chromatin Biology ◽  
Biology Research

Histone post-translational modification (PTM) antibodies are essential research reagents in chromatin biology. However, they suffer from variable properties and insufficient documentation of quality. Antibody manufacturers and vendors should provide detailed lot-specific documentation of quality, rendering further quality checks by end-customers unnecessary. A shift from polyclonal antibodies towards sustainable reagents like monoclonal or recombinant antibodies or histone binding domains would help to improve the reproducibility of experimental work in this field.

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