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Gene Review:

Nlp - Nucleoplasmin

Drosophila melanogaster

Synonyms: CG7917, CRP1, Chromatin decondensation protein 1, Crp1, Dmel\CG7917, ...

Crevel, G. et al., Ito, T. et al., Renault, L. et al., Hedley, M.L. et al., Hill, R.J. et al.

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High impact information on Nlp

Mutations in the gene affect pre-messenger RNA processing and transport, mating, initiation of mitosis and chromatin decondensation, suggesting that RCC1 is important in the control of nucleo-cytoplasmic transport and the cell cycle [1].
The first step is transport across the nuclear envelope via the nucleoplasmin-like NLS, while the second step is association with components in the speckled domain via the RS dipeptide sequence [2].
These and other data collectively suggest that dNLP may participate in parallel with other histone-binding proteins such as dNAP-1 in the assembly of chromatin [3].
ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster [3].
CRP1 is able to substitute for nucleoplasmin in Xenopus egg extract-mediated sperm chromatin decondensation [4].

Biological context of Nlp

CRP1 is encoded by one or several closely related genes found at a single locus, position 99A on the right arm of chromosome 3 [4].
CRP1 mRNA is expressed throughout Drosophila development; it is highest during oogenesis and early embryogenesis. mRNA levels correlate closely with levels of protein expression measured previously [4].
Alignment of deduced amino acid sequence with published sequences of other proteins revealed strong homologies to Xenopus nucleoplasmin and NO38 [4].

Other interactions of Nlp

We observed that dNAP-1, but not dNLP, was able to promote the decondensation of sperm chromatin [3].

Analytical, diagnostic and therapeutic context of Nlp

Results of chemical crosslinking indicate that CRP1 is either tetrameric or pentameric; similar ambiguity was revealed by direct visualization using scanning transmission electron microscopy [4].
Scanning transmission electron microscopic examination after negative staining revealed that CRP1 and Xenopus nucleoplasmin are morphologically similar [4].
The immunofluorescence over puffs, albeit lower than that over bands and interbands, indicates that chromatin decondensation can occur without complete loss of H1 in these structures [5].

References

The 1.7 A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Renault, L., Nassar, N., Vetter, I., Becker, J., Klebe, C., Roth, M., Wittinghofer, A. Nature (1998) [Pubmed]
An amino acid sequence motif sufficient for subnuclear localization of an arginine/serine-rich splicing factor. Hedley, M.L., Amrein, H., Maniatis, T. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster. Ito, T., Tyler, J.K., Bulger, M., Kobayashi, R., Kadonaga, J.T. J. Biol. Chem. (1996) [Pubmed]
Molecular and cellular characterization of CRP1, a Drosophila chromatin decondensation protein. Crevel, G., Huikeshoven, H., Cotterill, S., Simon, M., Wall, J., Philpott, A., Laskey, R.A., McConnell, M., Fisher, P.A., Berrios, M. J. Struct. Biol. (1997) [Pubmed]
Bands, interbands and puffs in native Drosophila polytene chromosomes are recognized by a monoclonal antibody to an epitope in the carboxy-terminal tail of histone H1. Hill, R.J., Watt, F., Wilson, C.M., Fifis, T., Underwood, P.A., Tribbick, G., Geysen, H.M., Thomas, J.O. Chromosoma (1989) [Pubmed]

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