The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding.
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.
Namboodiri
V M Haridasan
VM
Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA 02118, USA.
Dutta
Shuchismita
S
Akey
Ildikó V
IV
Head
James F
JF
Akey
Christopher W
CW
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D004330:Drosophila / Q000737:chemistry* / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D029543:Nucleocytoplasmic Transport Proteins; D016415:Sequence Alignment; D013696:Temperature
D006657:Histones; C119720:NUP42 protein, human; D009687:Nuclear Proteins; D029543:Nucleocytoplasmic Transport Proteins