Nucleoplasmin, the first identified molecular chaperone[1] is a thermostable acidic protein with a pentameric structure.

The protein was first isolated from Xenopus species[2][3][4] The pentameric protein participates in various significant cellular activities like sperm chromatin remodeling, nucleosome assembly, genome stability, ribosome biogenesis, DNA duplication and transcriptional regulation.

[4][5] During the assembly of regular nucleosomal arrays, these nucleoplasmins transfer the DNA to them by binding to the histones.

This reaction requires ATP.

[2][6][7][8] Humans express three members of the nucleoplasmin family: This protein-related article is a stub.