Nucleoplasmin
| Nucleoplasmin family | |
|---|---|
 Illustration of the structure of nucleoplasmin | |
| Identifiers | |
| Symbol | NPM |
| InterPro | IPR004301 |
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]
Functions
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]
Human proteins
Humans express three members of the nucleoplasmin family:
- Nucleophosmin (NPM1)
- Nucleoplasmin 2 (NPM2)
- Nucleoplasmin 3 (NPM3)
References
- PMID 1983266.
- ^ PMID 7779801.
- PMID 6814762.
- ^ a b Tejun S, Yaozhou Z (2007). "Nucleoplasmin, an Important Nuclear Chaperone". Chinese Journal of Biochemistry and Molecular Biology. 23 (9): 718–723.
- PMID 17187372.
- ^ "Nucleoplasmin-like core domain superfamily". Superfamily 1.75, HMM Library and Genome Assignment Server.
- PMID 24121686.
- ^ "Nucleoplasmin family". InterPro. EMBL-EBI, Wellcome Trust Genome Campus,European Molecular Biology Laboratory.
Further reading
- Philpott A, Leno GH (May 1992). "Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts". Cell. 69 (5): 759–767. PMID 1591776.
- Laskey RA, Mills AD, Philpott A, Leno GH, Dilworth SM, Dingwall C (March 1993). "The role of nucleoplasmin in chromatin assembly and disassembly". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 339 (1289): 263–269. PMID 8098530.
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