Biology:Nucleoplasmin

From HandWiki
Short description: InterPro Family
Nucleoplasmin family
Drawing of the pentameric structure
Illustration of the structure of nucleoplasmin
Identifiers
SymbolNPM
InterProIPR004301

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

  1. "Nucleoplasmin: the archetypal molecular chaperone". Seminars in Cell Biology 1 (1): 11–17. February 1990. PMID 1983266. 
  2. 2.0 2.1 "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. June 1995. doi:10.1021/bi00023a001. PMID 7779801. 
  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. 4.0 4.1 "Nucleoplasmin, an Important Nuclear Chaperone". Chinese Journal of Biochemistry and Molecular Biology 23 (9): 718–723. 2007. http://cjbmb.bjmu.edu.cn/EN/abstract/abstract17664.shtml. 
  5. "New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones". BioEssays 29 (1): 49–59. January 2007. doi:10.1002/bies.20512. PMID 17187372. 
  6. "Nucleoplasmin-like core domain superfamily". Superfamily 1.75, HMM Library and Genome Assignment Server. http://supfam.org/SUPERFAMILY/cgi-bin/scop.cgi?sunid=69203. 
  7. "The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones". Nucleic Acids Research 42 (2): 1311–1325. January 2014. doi:10.1093/nar/gkt899. PMID 24121686. 
  8. "Nucleoplasmin family". InterPro. EMBL-EBI, Wellcome Trust Genome Campus,European Molecular Biology Laboratory. http://www.ebi.ac.uk/interpro/entry/IPR004301. 

Further reading