We are analyzing https://link.springer.com/article/10.1007/s12551-022-01014-9.

Title:
Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones | Biophysical Reviews
Description:
Advances in structural analysis by cryogenic electron microscopy (cryo-EM) and X-ray crystallography have revealed the tertiary structures of various chromatin-related proteins, including transcription factors, RNA polymerases, nucleosomes, and histone chaperones; however, the dynamic structures of intrinsically disordered regions (IDRs) in these proteins remain elusive. Recent studies using nuclear magnetic resonance (NMR), together with molecular dynamics (MD) simulations, are beginning to reveal dynamic structures of the general transcription factor TFIIH complexed with target proteins including the general transcription factor TFIIE, the tumor suppressor p53, the cell cycle protein DP1, the DNA repair factors XPC and UVSSA, and three RNA polymerases, in addition to the dynamics of histone tails in nucleosomes and histone chaperones. In complexes of TFIIH, the PH domain of the p62 subunit binds to an acidic string formed by the IDR in TFIIE, p53, XPC, UVSSA, DP1, and the RPB6 subunit of three RNA polymerases by a common interaction mode, namely extended string-like binding of the IDR on the positively charged surface of the PH domain. In the nucleosome, the dynamic conformations of the N-tails of histones H2A and H2B are correlated, while the dynamic conformations of the N-tails of H3 and H4 form a histone tail network dependent on their modifications and linker DNA. The acidic IDRs of the histone chaperones of FACT and NAP1 play important roles in regulating the accessibility to histone proteins in the nucleosome.
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Keywords {🔍}

article, google, scholar, cas, nishimura, histone, biol, domain, cell, dna, structure, mol, nucleosome, binding, protein, transcription, structural, tfiih, fact, chem, repair, subunit, sci, human, rna, chromatin, factor, dnabinding, complex, proteins, okuda, res, usa, proc, natl, httpsdoiorgpnas, transactivation, nucleic, acad, httpsdoiorgjmolcel, acids, nature, interaction, chaperone, httpsdoiorgs, nmr, dynamics, nakamura, disordered, assembly,

Topics {✒️}

transcriptional activator/p300/nap1/h1 pathway post-translational modifications determine helix-turn-helix-related motif ompr dna-binding/transactivation domains double-stranded dna-binding surface month download article/chapter nap1-dependent h2a–h2b deposition c-myb dna-binding domain phob dna-binding/transctivation domain c-myb protooncogene product histone methylated-lysine residues single-stranded dna mimicry single-stranded dna mimics transcription-coupled repair subpathways regulate transcription-coupled repair myb dna-binding domains dna repair-deficient diseases dna-dependent rna polymerase differentially isotope-labeled nucleosomes c-terminal acidic domain h2a–h2b histone chaperone histone h2a–h2b chaperone cdc2-related protein p40mo15 myb dna-binding domain time-resolved nmr spectroscopy amino-terminal histone tails gene-specific h1 eviction transcription-blocking dna damage nmr-restrained molecular dynamics phosphorylation-coupled intramolecular dynamics histone tail network intrinsically disordered protein intrinsically disordered proteins cryo-electron microscopy structure transcription factor iih chromatin-related proteins nucleotide excision repairosome c-terminal domain full article pdf reveal dynamic structures intrinsically disordered regions intrinsically disordered region histone chaperone fact rna polymerase ii nap1-related protein 1 privacy choices/manage cookies amino-terminal domain basic transcription factor n-terminal tails phosphorylated transactivation domain

Questions {❓}

Formosa T, Winston F (2020) The role of FACT in managing chromatin: disruption, assembly, or repair?

Schema {🗺️}

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