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]
| Nucleoplasmin family | |
|---|---|
Illustration of the structure of nucleoplasmin | |
| Identifiers | |
| Symbol | NPM |
| InterPro | IPR004301 |
Functions
editThe 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
editHumans express three members of the nucleoplasmin family:
- Nucleophosmin (NPM1)
- Nucleoplasmin 2 (NPM2)
- Nucleoplasmin 3 (NPM3)
References
edit- ^ Dingwall C, Laskey RA (February 1990). "Nucleoplasmin: the archetypal molecular chaperone". Seminars in Cell Biology. 1 (1): 11–17. PMID 1983266.
- ^ a b Rice P, Garduño R, Itoh T, Katagiri C, Ausio J (June 1995). "Nucleoplasmin-mediated decondensation of Mytilus sperm chromatin. Identification and partial characterization of a nucleoplasmin-like protein with sperm-nuclei decondensing activity in Mytilus californianus". Biochemistry. 34 (23): 7563–7568. doi:10.1021/bi00023a001. PMID 7779801.
- ^ Dingwall C, Sharnick SV, Laskey RA (September 1982). "A polypeptide domain that specifies migration of nucleoplasmin into the nucleus". Cell. 30 (2): 449–458. doi:10.1016/0092-8674(82)90242-2. 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.
- ^ Frehlick LJ, Eirín-López JM, Ausió J (January 2007). "New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones". BioEssays. 29 (1): 49–59. doi:10.1002/bies.20512. PMID 17187372.
- ^ "Nucleoplasmin-like core domain superfamily". Superfamily 1.75, HMM Library and Genome Assignment Server.
- ^ Ramos I, Fernández-Rivero N, Arranz R, Aloria K, Finn R, Arizmendi JM, et al. (January 2014). "The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones". Nucleic Acids Research. 42 (2): 1311–1325. doi:10.1093/nar/gkt899. PMC 3902905. PMID 24121686.
- ^ "Nucleoplasmin family". InterPro. EMBL-EBI, Wellcome Trust Genome Campus,European Molecular Biology Laboratory.
Further reading
edit- Philpott A, Leno GH (May 1992). "Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts". Cell. 69 (5): 759–767. doi:10.1016/0092-8674(92)90288-n. 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. doi:10.1098/rstb.1993.0024. JSTOR 55822. PMID 8098530.
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