Related Experiment Video
Updated: Aug 13, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
Nuclear chaperones
A Philpott1, T Krude, R A Laskey
1Department of Oncology, University of Cambridge, Wellcome Trust Centre for the Study of Molecular Mechanisms in Disease, Cambridge Institute for Medical Research, Wellcome/MRC Building, Addenbrooke's Hospital, Hills Road, Cambridge, CB2 2XY, UK.
Abstract:
We discuss nuclear chaperones that bind correctly folded protein subunits and mediate molecular interactions, particularly between proteins and nucleic acids. The charge of these chaperones helps to prevent non-specific electrostatic interactions between the components. Thus, an ordered assembly of macromolecular complexes is mediated, most notably in the formation and maintenance of chromatin, though similar principles are likely to apply in ribonucleoprotein assembly. Here, we discuss roles for nuclear chaperones in mediating nucleosome assembly and remodelling during DNA replication and transcription, and upon fertilisation.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Nuclear Protein Sorting
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Nuclear Export
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Regulation of Nuclear Protein Sorting
Molecular Chaperones and Protein Folding
The...
Bacterial Protein Maturation

