| Structural highlights
Function
[NLP_DROME] Binds to core histones and functions in the ATP-facilitated assembly of approximately regularly spaced nucleosomal arrays. May participate in parallel with other histone-binding proteins such as NAP-1.[1] [2] Isoform 2 is inactive for chromatin assembly. In vitro it appears to form a high molecular mass aggregate with the core histones.[3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The nucleoplasmin-like protein from Drosophila (dNLP) functions as a chaperone for core histones and may remodel chromatin in embryos. We now report the crystal structure of a dNLP-core pentamer at 1.5 A resolution. The monomer has an eight-stranded, beta barrel topology that is similar to nucleoplasmin (Np). However, a signature beta hairpin is tucked in along the lateral surface of the dNLP-core pentamer, while it extends outward in the Np-core decamer. Drosophila NLP and Np both assemble histone octamers. This process may require each chaperone to form a decamer, which would create symmetric binding sites for the histones. Conformational differences between dNLP and Np may reflect their different oligomeric states, while a conserved, nonpolar subunit interface may allow conformational plasticity during histone binding.
The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding.,Namboodiri VM, Dutta S, Akey IV, Head JF, Akey CW Structure. 2003 Feb;11(2):175-86. PMID:12575937[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ito T, Tyler JK, Bulger M, Kobayashi R, Kadonaga JT. ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster. J Biol Chem. 1996 Oct 4;271(40):25041-8. PMID:8798787
- ↑ Crevel G, Huikeshoven H, Cotterill S, Simon M, Wall J, Philpott A, Laskey RA, McConnell M, Fisher PA, Berrios M. Molecular and cellular characterization of CRP1, a Drosophila chromatin decondensation protein. J Struct Biol. 1997 Feb;118(1):9-22. PMID:9087911 doi:http://dx.doi.org/S1047-8477(96)93836-8
- ↑ Ito T, Tyler JK, Bulger M, Kobayashi R, Kadonaga JT. ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster. J Biol Chem. 1996 Oct 4;271(40):25041-8. PMID:8798787
- ↑ Crevel G, Huikeshoven H, Cotterill S, Simon M, Wall J, Philpott A, Laskey RA, McConnell M, Fisher PA, Berrios M. Molecular and cellular characterization of CRP1, a Drosophila chromatin decondensation protein. J Struct Biol. 1997 Feb;118(1):9-22. PMID:9087911 doi:http://dx.doi.org/S1047-8477(96)93836-8
- ↑ Namboodiri VM, Dutta S, Akey IV, Head JF, Akey CW. The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding. Structure. 2003 Feb;11(2):175-86. PMID:12575937
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