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
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Further reading
- Philpott, Anna, and Gregory H. Leno. "Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts." Cell 69.5 (1992): 759-767.
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- Dingwall, C., and R. A. Laskey. "Nucleoplasmin: the archetypal molecular chaperone." Seminars in cell biology. Vol. 1. No. 1. 1990.
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