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]

References

  1. C, Dingwall; RA., Laskey (Feb 1990). "Nucleoplasmin: the archetypal molecular chaperone.". Seminars in Cell Biology. pp. 11–17.
  2. 1 2 "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. ACS publications. June 1995. pp. 7563–7568. doi:10.1021/bi00023a001.
  3. "A polypeptide domain that specifies migration of nucleoplasmin into the nucleus". Cell. 30 (2): 449–458. September 1982. doi:10.1016/0092-8674(82)90242-2. PMID 6814762.
  4. 1 2 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. pp. 49–59. doi:10.1002/bies.20512.
  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. doi:10.1093/nar/gkt899.
  8. "InterPro". EMBL-EBI, Wellcome Trust Genome Campus,European Molecular Biology Laboratory.

Further reading


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