Dynamic Remodeling of Transcription Complexes by Molecular Chaperones

Dynamic Remodeling of Transcription Complexes by Molecular Chaperones

The assembly and disassembly of macromolecular transcription complexes represents a key step in the regulation of gene expression. For inducible responses to hormones and stress, different combinations of molecular chaperones govern the activities of intracellular hormone receptors and heat shock transcription factor. Through their capacity to remodel the conformation of these activators, chape...

Disassembly of transcriptional regulatory complexes by molecular chaperones.

Many biological processes are initiated by cooperative assembly of large multicomponent complexes; however, mechanisms for modulating or terminating the actions of these complexes are not well understood. For example, hormone-bound intracellular receptors (IRs) nucleate formation of transcriptional regulatory complexes whose actions cease promptly upon hormone withdrawal. Here, we show that the...

Dynamic regulation of transcription factors by nucleosome remodeling

The chromatin landscape and promoter architecture are dominated by the interplay of nucleosome and transcription factor (TF) binding to crucial DNA sequence elements. However, it remains unclear whether nucleosomes mobilized by chromatin remodelers can influence TFs that are already present on the DNA template. In this study, we investigated the interplay between nucleosome remodeling, by eithe...

Polyomavirus T antigens: molecular chaperones for multiprotein complexes.

Molecular Chaperones

In most cases proteins fold spontaneously under physiological conditions and do not require any external assistance. This has become evident since the experiments on ribonuclease A conducted by Anfinsen in ‘50s and ‘60s. The list of such “successful” folders has grown since and now includes many two-state proteins catalogued in Folding & Design 3, R81. These proteins fold rapidly and reliably t...