5G2E

Structure of the Nap1 H2A H2B complex

Summary for 5G2E

• Entry DOI: 10.2210/pdb5g2e/pdb
• Descriptor: NUCLEOSOME ASSEMBLY PROTEIN, HISTONE H2A TYPE 1, HISTONE H2B 1.1 (3 entities in total)
• Functional Keywords: dna binding protein, nucleosome assembly protein 1, histone, h2a-h2b, chromatin, nucleosome assembly
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm: P25293; Nucleus: P06897 P02281
• Total number of polymer chains: 24
• Total formula weight: 571415.48

Authors

AguilarGurrieri, C.,Larabi, A.,Vinayachandran, V.,Patel, N.A.,Yen, K.,Reja, R.,Ebong, I.O.,Schoehn, G.,Robinson, C.V.,Pugh, B.F.,Panne, D. (deposition date: 2016-04-07, release date: 2016-08-03, Last modification date: 2024-01-10)

Primary citation

Aguilar-Gurrieri, C.,Larabi, A.,Vinayachandran, V.,Patel, N.A.,Yen, K.,Reja, R.,Ebong, I.,Schoehn, G.,Robinson, C.V.,Pugh, B.F.,Panne, D.
Structural Evidence for Nap1-Dependent H2A-H2B Deposition and Nucleosome Assembly.
Embo J., 35:1465-, 2016

PubMed Abstract: Nap1 is a histone chaperone involved in the nuclear import of H2A-H2B and nucleosome assembly. Here, we report the crystal structure of Nap1 bound to H2A-H2B together with in vitro and in vivo functional studies that elucidate the principles underlying Nap1-mediated H2A-H2B chaperoning and nucleosome assembly. A Nap1 dimer provides an acidic binding surface and asymmetrically engages a single H2A-H2B heterodimer. Oligomerization of the Nap1-H2A-H2B complex results in burial of surfaces required for deposition of H2A-H2B into nucleosomes. Chromatin immunoprecipitation-exonuclease (ChIP-exo) analysis shows that Nap1 is required for H2A-H2B deposition across the genome. Mutants that interfere with Nap1 oligomerization exhibit severe nucleosome assembly defects showing that oligomerization is essential for the chaperone function. These findings establish the molecular basis for Nap1-mediated H2A-H2B deposition and nucleosome assembly.

PubMed: 27225933
DOI: 10.15252/EMBJ.201694105

Experimental method

X-RAY DIFFRACTION (6.7 Å)