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Papers In Press, published online ahead of print August 19, 2003
Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870
Corresponding Author: kluger{at}lamar.colostate.edu
The yeast nucleosome assembly protein 1 (yNAP1) participates in many diverse activities, such as the assembly of newly synthesized DNA into chromatin, and the rearrangement of nucleosomes during transcriptional activation. yNAP1 does not require ATP hydrolysis to perform these functions. Using recombinant histone complexes, we show that yNAP1 has a preference for binding the (H3-H4)2 tetramer over the (H2A-H2B) dimer. We find that the loss of the histone tails abrogates this preference for H3 and H4, and demonstrate a direct interaction between yNAP1 and the N-terminal tails of H3 and H4. In the absence of the acidic C-terminal domain, yNAP1 binds stoichiometrically to each of the four histone-fold domains, without distinguishing between the different histone sub-complexes. We provide evidence that the acidic carboxyl terminal region of yNAP1, while dispensable for nucleosome assembly in vitro, contributes to binding via structure-independent electrostatic interactions. Our results are consistent with recent mechanistic investigations of NAP1, and expand our understanding of the histone-chaperone family of assembly factors.
J. Biol. Chem, 10.1074/jbc.M305636200
Submitted on May 29, 2003
Revised on August 19, 2003
Accepted on August 19, 2003
Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino terminal histone tails
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