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 1 (1). 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. 34(23). 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 29 (1). 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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