PDBsum entry 4xzq

Structural protein/DNA

PDB id: 4xzq

Contents

Protein chains

98 a.a.

79 a.a.

106 a.a.

93 a.a.

DNA/RNA

Waters ×99

PDB id:

4xzq

Name:

Structural protein/DNA

Title:

Nucleosome disassembly by rsc and swi/snf is enhanced by h3 acetylation near the nucleosome dyad axis

Structure:

Histone h3.2. Chain: a, e. Fragment: residues 39-136. Engineered: yes. Other_details: h3 acetylated at lysine 115. Histone h4. Chain: b, f. Fragment: residues 25-103. Engineered: yes.

Source:

Xenopus laevis. African clawed frog. Organism_taxid: 8355. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hist1h2aj, loc494591. Synthetic: yes. Homo sapiens. Organism_taxid: 9606.

Resolution:

2.40Å R-factor: 0.256 R-free: 0.300

Authors:

M.L.Dechassa,K.Luger,N.Chatterjee,J.A.North,M.Manohar,R.Prasad, J.J.Ottessen,M.G.Poirier,B.Bartholomew

Key ref:

N.Chatterjee et al. (2015). Histone Acetylation near the Nucleosome Dyad Axis Enhances Nucleosome Disassembly by RSC and SWI/SNF. Mol Cell Biol, 35, 4083-4092. PubMed id: 26416878 DOI: 10.1128/MCB.00441-15

Date:

04-Feb-15 Release date: 14-Oct-15

Protein chains

P84233  (H32_XENLA) -  Histone H3.2 from Xenopus laevis

Seq: 136 a.a.

Struc: 98 a.a.*

Protein chains

P62799  (H4_XENLA) -  Histone H4 from Xenopus laevis

Seq: 103 a.a.

Struc: 79 a.a.

Protein chains

P06897  (H2A1_XENLA) -  Histone H2A type 1 from Xenopus laevis

Seq: 130 a.a.

Struc: 106 a.a.*

Protein chains

P02281  (H2B11_XENLA) -  Histone H2B 1.1 from Xenopus laevis

Seq: 126 a.a.

Struc: 93 a.a.

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DNA/RNA chains

A-T-C-A-A-T-A-T-C-C-A-C-C-T-G-C-A-G-A-T-A-C-T-A-C-C-A-A-A-A-G-T-G-T-A-T-T-T-G- 147 bases

A-T-C-A-A-T-A-T-C-C-A-C-C-T-G-C-A-G-A-T-A-C-T-A-C-C-A-A-A-A-G-T-G-T-A-T-T-T-G- 147 bases

DOI no: 10.1128/MCB.00441-15

Mol Cell Biol 35:4083-4092 (2015)

PubMed id: 26416878

Histone Acetylation near the Nucleosome Dyad Axis Enhances Nucleosome Disassembly by RSC and SWI/SNF.

N.Chatterjee, J.A.North, M.L.Dechassa, M.Manohar, R.Prasad, K.Luger, J.J.Ottesen, M.G.Poirier, B.Bartholomew.

ABSTRACT

Signaling associated with transcription activation occurs through posttranslational modification of histones and is best exemplified by lysine acetylation. Lysines are acetylated in histone tails and the core domain/lateral surface of histone octamers. While acetylated lysines in histone tails are frequently recognized by other factors referred to as "readers," which promote transcription, the mechanistic role of the modifications in the lateral surface of the histone octamer remains unclear. By using X-ray crystallography, we found that acetylated lysines 115 and 122 in histone H3 are solvent accessible, but in biochemical assays they appear not to interact with the bromodomains of SWI/SNF and RSC to enhance recruitment or nucleosome mobilization, as previously shown for acetylated lysines in H3 histone tails. Instead, we found that acetylation of lysines 115 and 122 increases the predisposition of nucleosomes for disassembly by SWI/SNF and RSC up to 7-fold, independent of bromodomains, and only in conjunction with contiguous nucleosomes. Thus, in combination with SWI/SNF and RSC, acetylation of lateral surface lysines in the histone octamer serves as a crucial regulator of nucleosomal dynamics distinct from the histone code readers and writers.