1P34

Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

Summary for 1P34

• Entry DOI: 10.2210/pdb1p34/pdb
• Related: 1AOI 1F66 1ID3 1KX3 1KX4 1KX5 1P3A 1P3B 1P3F 1P3G 1P3I 1P3K 1P3L 1P3M 1P3O 1P3P
• Descriptor: Palindromic 146bp Human Alpha-Satellite DNA fragment, Histone H3, Histone H4, ... (6 entities in total)
• Functional Keywords: sin mutants, nucleosome core particle, chromatin, protein/dna interaction, structural protein-dna complex, structural protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P62799 P02281
• Total number of polymer chains: 10
• Total formula weight: 198784.42

Authors

Muthurajan, U.M.,Bao, Y.,Forsberg, L.J.,Edayathumangalam, R.S.,Dyer, P.N.,White, C.L.,Luger, K. (deposition date: 2003-04-17, release date: 2004-02-24, Last modification date: 2023-08-16)

Primary citation

Muthurajan, U.M.,Bao, Y.,Forsberg, L.J.,Edayathumangalam, R.S.,Dyer, P.N.,White, C.L.,Luger, K.
Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions
EMBO J., 23:260-271, 2004

PubMed Abstract: Here we describe 11 crystal structures of nucleosome core particles containing individual point mutations in the structured regions of histones H3 and H4. The mutated residues are located at the two protein-DNA interfaces flanking the nucleosomal dyad. Five of the mutations partially restore the in vivo effects of SWI/SNF inactivation in yeast. We find that even nonconservative mutations of these residues (which exhibit a distinct phenotype in vivo) have only moderate effects on global nucleosome structure. Rather, local protein-DNA interactions are disrupted and weakened in a subtle and complex manner. The number of lost protein-DNA interactions correlates directly with an increased propensity of the histone octamer to reposition with respect to the DNA, and with an overall destabilization of the nucleosome. Thus, the disruption of only two to six of the approximately 120 direct histone-DNA interactions within the nucleosome has a pronounced effect on nucleosome mobility and stability. This has implications for our understanding of how these structures are made accessible to the transcription and replication machinery in vivo.

PubMed: 14739929
DOI: 10.1038/sj.emboj.7600046

Experimental method

X-RAY DIFFRACTION (2.7 Å)