Nuclear chaperones.
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.
Philpott
A
A
Department 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.
Krude
T
T
Laskey
R A
RA
D000818:Animals; D002843:Chromatin / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D046911:Macromolecular Substances; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism* / Q000502:physiology*; D009687:Nuclear Proteins / Q000378:metabolism / Q000502:physiology*; D056489:Nucleoplasmins; D009698:Nucleoproteins / Q000096:biosynthesis; D010750:Phosphoproteins / Q000378:metabolism / Q000502:physiology
D002843:Chromatin; D046911:Macromolecular Substances; D018832:Molecular Chaperones; D009687:Nuclear Proteins; D056489:Nucleoplasmins; D009698:Nucleoproteins; D010750:Phosphoproteins