Histones (H) are the major protein components of chromatin which help to pack the DNA in the nucleosomes. H2A, H2B, H3 and H4 are core histones while H1 and H5 are linker histones[1]. The nucleosome is the repeated unit of the chromatin consisting of a core which contains 8 histone molecules (two copies of H2A, H2B, H3 and H4) wrapped by ca. 140 base pairs of DNA[2]. The chromatin is made of nucleosome cores separated by a linker region of upto 80 base pairs of DNA associated with histones H1 and H5.
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3D Structures of histone3D Structures of histone
Updated on 09-January-2017
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- Histone
- 1yqa – yH1 (mutant) – yeast – NMR
- 1uss, 1ust, 1uhm – yH1 globular domain - NMR
- 1ghc – cH1 – chicken - NMR
- 2xd7, 1zr3, 1zr5, 2fxk – hH2A macro domain – human
- 4cay – hH2A +H2B
- 1yd9 – H2A macro domain – rat
- 1ku5 – HPHA – Pyrococcus horikoshii
- 1b67, 1b6w, 1a7w, 1hta – MfHMFA – Methanococcus fervidus
- 1bfm – MfHB - NMR
- 1f1e – H – Methanopyrus kandleri
- 1hst – cH5
- 3iid, 3iif – H2A macro domain + ADP-ribose
- 2g9a, 2g99, 2h13 – H3 + WD-repeat protein
- 1pfb – H3 + polycomb protein – Strongylocentrus purpuratus
- Nucleosome core
- 3r45 - hH4 + H3-like centromeric protein + Holliday junction recognition protein
- 3nqj, 3nqu - hH4 + H3-like centromeric protein
- 4h9n, 4h9o, 4h9p, 4h9q, 4h9r, 4h9s, 4hga - XlH3.3 (mutant) + H4 + death domain-associated protein 6
- 3qzs, 3qzt – XlH4 + nucleosome-remodeling factor subunit BPTF – Xenopus laevis
- 2io5 - XlH3.1 + H4 + anti-silencing protein
- 4eo5 - XlH3.2 (mutant) + H4 (mutant) + histone chaperone ASF1
- 4ld9 - XlH3.2 + H4 + H2A + H2B + widom sequence reverse + SIR3
- 2yfv, 2yfw - H4 + H3-like centromeric protein + SCM3 – Kluyveromyces lactis
- 2l5a - yH4/H3-like centromeric protein/SCM3
- 2jss - yH2A/H2B + CHZ1 – NMR
- 2hue - yH3 + H4 + anti-silencing protein
- 2xql, 3c9k - cH3.2 + H4 + H2A + H2B – EM
- 4uuz – DmH3 + H4 + DNA replication licensing factor – Drosophila melanogaster
- Nucleosome core + DNA
- 3an2, 4x23 – hH4 + H2A + H2B + H3-like centromeric protein + DNA
- 3av1, 2av2, 3av2, 3waa, 3wa9, 3w99, 3w98, 3w97, 3w96 – hH3.2 + H4 + H2A + H2B + DNA
- 3a6n, 3afa, 2cv5 - hH3.1 + H4 + H2A + H2B + DNA
- 3ayw, 3aze, 3azf, 3azg, 3azh - hH3.1 (mutant) + H4 + H2A + H2B + DNA
- 3azi, 3azj, 3azk, 3azl, 3azm, 3azn - hH3.1 + H4 (mutant) + H2A + H2B + DNA
- 3mnn, 3o62, 3lz0, 3lz1, 3lel, 3kuy, 3c1b, 3c1c, 2nzd, 2fj7, 1zbb, 1s32, 1p34, 1p3a, 1p3b, 1p3f, 1p3g, 1p3i, 1p3k, 1p3l, 1p3m, 1p3o, 1p3p, 1m18, 1m19, 1m1a, 1kx3, 1kx4, 1kx5, 1aoi, 3reh, 3rei, 3rej, 3rek, 3rel, 3ut9, 3uta, 3utb - XlH3.2 + H4 + H2A + H2B + DNA
- 2f8n - XlH3.1 + H4 + H2A + H2B + H3 + H2A macro domain + DNA
- 1zla – XlH3 + H4 + H2A + H2B + H3 + antigen + DNA
- 3mgp, 3mgq, 3mgr, 3mgs, 3lja, 3b6f, 3b6g, 4j8u, 4j8v, 4j8w, 4j8x, 4kgc - XlH3.2 + H4 + H2A + H2B + metal ion + DNA
- 3kxb - XlH3.2 (mutant) + H4 + H2A + H2B (mutant) + DNA
- 3kwq - XlH3.2 (mutant) + H4 + H2A + H2B + DNA
- 3mvd - XlH3.2 + H4 + H2A + H2B + regulator of chromosome condensation + DNA
- 3tu4 - XlH3.2 + H4 + H2A + H2B + regulatory protein SIR3 + DNA
- 4r8p - XlH3.2 + H4 + H2A + H2B + polycomb complex protein + ring finger protein + DNA
- 1id3 - yH3 + H4 + H2A + H2B + DNA
- 4jjn, 4kud - yH3 + H4 + H2A.2 + H2B.2 + SIR3 + DNA
- 2aro, 1tzy, 1hq3, 2hio, 1hio - cH3 + H4 + H2A + H2B
- 1eqz - cH3 + H4 + H2A + H2B + DNA
- 2pyo, 2nqb, 3nqb - DmH3 + H4 + H2A + H2B + DNA
- 4x23 - DmH3 + H4 + H2A + H2B + centromeric protein C + DNA
- 1u35 - mH3.1 + H2A + H2B + His2A macro domain + DNA – mouse
- 1f66 - XlH3 + mH4 + hH2A + XlH2B + DNA
ReferencesReferences
- ↑ Marino-Ramirez L, Kann MG, Shoemaker BA, Landsman D. Histone structure and nucleosome stability. Expert Rev Proteomics. 2005 Oct;2(5):719-29. PMID:16209651 doi:http://dx.doi.org/10.1586/14789450.2.5.719
- ↑ Kornberg RD. Chromatin structure: a repeating unit of histones and DNA. Science. 1974 May 24;184(4139):868-71. PMID:4825889
