Chromatin Remodeling
Our nucleosomal DNA is exposed to constant changes in structure, composition and positioning of nucleosomes in order to expose entire regions of a chromosome or render them inaccessible instead. This process is called chromatin remodeling - the highest level of transcription regulation in eukaryotes.
Covalent histone modifications by specific enzymes, and ATP-dependent chromatin remodeling complexes which move, eject or restructure nucleosomes are responsible for chromatin remodeling. Remodeling of chromatin imparts an epigenetic regulatory role in several key biological processes for example DNA damage repair or apoptosis.
Antibodies for Chromatin Remodeling
Covalent Histone-Modifying Complexes
Specific protein complexes, like histone acetyltransferases (HATs), deacetylases, methyltransferases, and kinases, known as histone-modifying complexes catalyze addition or removal of various chemical elements on histones. Such modifications affect the binding affinity between histones and DNA, and thus loosening or tightening the condensed DNA wrapped around histones, e.g., Methylation of specific lysine residues in H3 and H4 causes further condensation of DNA around histones, and thereby prevents binding of transcription factors to the DNA that lead to gene repression. On the contrary, histone acetylation relaxes chromatin condensation and exposes DNA for TF binding, leading to increased gene expression.
Antibodies for ATP-Dependent Chromatin Remodeling and Covalent Histone-Modifying Complexes
ATP-Dependent Chromatin Remodeling
There are at least five families of chromatin remodelers in eukaryotes: SWI/SNF, ISWI, NuRD/Mi-2/CHD, INO80 and SWR1 with first two remodelers being very well studied so far, especially in the yeast model. Although all of remodelers share common ATPase domain, their functions are specific based on several biological processes. This is due to the fact that each remodeler complex has unique protein domains (Helicase, bromodomain, etc.) in their catalytic ATPase region and also has different recruited subunits.
The ISWI-family remodelers have been shown to play central roles in chromatin assembly after DNA replication and maintenance of higher-order chromatin structures. They organize nucleosome into proper bundle form and create equal spacing between nucleosomes, whereas SWI/SNF remodelers disorder nucleosomes.
INO80 and SWI/SNF-family remodelers participate in DNA double-strand break (DSB) repair and nucleotide-excision repair (NER) and thereby plays crucial role in TP53 mediated DNA-damage response. NuRD/Mi-2/CHD remodeling complexes primarily mediate transcriptional repression in the nucleus and are required for the maintenance of pluripotency of embryonic stem cells. Enzymes.
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References
- : "Structurally distinct Mre11 domains mediate MRX functions in resection, end-tethering and DNA damage resistance." in: Nucleic acids research, Vol. 46, Issue 6, pp. 2990-3008, (2019) (PubMed).
- : "ATM-dependent phosphorylation of MRE11 controls extent of resection during homology directed repair by signalling through Exonuclease 1." in: Nucleic acids research, Vol. 43, Issue 17, pp. 8352-67, (2015) (PubMed).
- : "Transcription Factors and DNA Repair Enzymes Compete for Damaged Promoter Sites." in: The Journal of biological chemistry, Vol. 291, Issue 11, pp. 5452-5460, (2016) (PubMed).
- : "ATP-dependent chromatin assembly is functionally distinct from chromatin remodeling." in: eLife, Vol. 2, pp. e00863, (2015) (PubMed).
- : "ATP-dependent chromatin remodeling during mammalian development." in: Development (Cambridge, England), Vol. 143, Issue 16, pp. 2882-97, (2017) (PubMed).
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