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A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1.

http://www.ncbi.nlm.nih.gov/pubmed/18068721

The histone chaperone nucleosome assembly protein 1 (NAP1) is implicated in histone shuttling as well as nucleosome assembly and disassembly. Under physiological conditions, NAP1 dimers exist in a mixture of various high-molecular-weight oligomers whose size may be regulated by the cell cycle-dependent concentration of NAP1. Both the functional and structural significance of the observed oligomers are unknown. We have resolved the molecular mechanism by which yeast NAP1 (yNAP1) dimers oligomerize by applying x-ray crystallographic, hydrodynamic, and functional approaches. We found that an extended beta-hairpin that protrudes from the compact core of the yNAP1 dimer forms a stable beta-sheet with beta-hairpins of neighboring yNAP1 dimers. Disruption of the beta-hairpin (whose sequence is conserved among NAP1 proteins in various species) by the replacement of one or more amino acids with proline results in complete loss of yNAP1 dimer oligomerization. The in vitro functions of yNAP1 remain unaffected by the mutations. We have thus identified a conserved structural feature of NAP1 whose function, in addition to presenting the nuclear localization sequence, appears to be the formation of higher-order oligomers.

Pubmed ID: 18068721 RIS Download

Mesh terms: Amino Acid Sequence | Amino Acid Substitution | Cell Cycle Proteins | Cell Nucleus | Crystallography, X-Ray | Dimerization | Fungal Proteins | Glutathione Transferase | Histones | Hydrogen-Ion Concentration | Models, Molecular | Molecular Chaperones | Molecular Sequence Data | Nuclear Proteins | Nucleosome Assembly Protein 1 | Osmolar Concentration | Proline | Protein Structure, Secondary | Protein Structure, Tertiary | Recombinant Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins

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