Nucleoplasmin

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)
gollark: No. You need something like GMP for bignums, but C has no operator overloading due to C bad.
gollark: Technically yes, practically not really I think; each connection has a bunch of state associated with it; the actual status of the TCP stream, and the random bytes the websocket data is XORed with (for entirely accursed reasons).
gollark: This is premature optimisation.
gollark: It doesn't actually matter unless you're writing some kind of hyperoptimized algorithm, which you aren't.
gollark: You can just use example.com, it has no SSL redirection.

References
  1. C, Dingwall; RA., Laskey (Feb 1990). "Nucleoplasmin: the archetypal molecular chaperone". Seminars in Cell Biology. 1 (1): 11–17. PMID 1983266.
  2. Rice, Philip; Garduno, Rafael; Itoh, Toru; Katagiri, Chiaki; Ausio, Juan (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.
  3. 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.
  4. Jun, SHUTe; Zhou, ZHANGYao (2007). "Nucleoplasmin, an Important Nuclear Chaperone". Chinese Journal of Biochemistry and Molecular Biol. 23 (9): 718–723.
  5. J. Frehlick, Lindsay; et al. (January 2007). "New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones". BioEssays. 29 (1): 49–59. doi:10.1002/bies.20512. PMID 17187372.
  6. "InterPro annotation". Superfamily 1.75, HMM Library and Genome Assignment Server.
  7. Ramos, Isbaal; et al. (2013). "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.
  8. "InterPro". EMBL-EBI, Wellcome Trust Genome Campus,European Molecular Biology Laboratory.

Further reading
  • Philpott, Anna; Leno, Gregory H. (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, R. A.; et al. (1993). "The Role of Nucleoplasmin in Chromatin Assembly and Disassembly". Philosophical Transactions: Biological Sciences. 339 (1289): 263–269. doi:10.1098/rstb.1993.0024. JSTOR 55822. PMID 8098530.
  • Dingwall, C.; Laskey, R. A. (1990). "Nucleoplasmin: the archetypal molecular chaperone". Seminars in Cell Biology. 1 (1).


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