Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
J Mol Evol
2005 Mar 01;603:354-64. doi: 10.1007/s00239-004-0193-6.
Show Gene links
Show Anatomy links
The hydrophobicity of the H3 histone fold differs from the hydrophobicity of the other three folds.
Silverman BD
.
???displayArticle.abstract???
The eukaryotic histone dimers, H3-H4 and H2A-H2B, are formed in the cytosol prior to being transported into the nucleus and assembled into the nucleosome. Residue side-chain distances from the interior of the histone dimers are obtained with an ellipsoidal spatial metric and structural information provided by X-ray analyses at atomic resolution of the nucleosome core particles. While the spatial hydrophobic moment profiles of the dimers are comparable with profiles obtained previously that characterize the hydrophobic core of single-chain, single-domain globular soluble proteins, correlation coefficients between the side-chain hydrophobicities and distances from the interior of the H3-H4 dimer and H2A-H2B dimer differ significantly. This difference is traced to the H3 histone fold, which segregates fewer hydrophobic residues within the protein interior than the three other folds. Examination of the correlation coefficient between residue hydrophobicity and side-chain distance from the dimer interior over local regions of the fold sequence shows that the region of reduced correlation is associated mainly with the residues at the carboxyl end of the H3 histone fold, the helical region of the fold involved in the H3-H3' binding of the (H3-H4)(2) tetramer of the nucleosome. Hydrophobic interactions apparently contribute to the binding of this fourfold helical bundle and this evolutionary requirement may trade off against the requirement for H3-H4 dimer stability. The present results provide a different view than previously proposed, albeit of similar origin, to account for the reduced stability of the H3-H4 dimer compared with the H2A-H2B dimer.
Akey,
Histone chaperones and nucleosome assembly.
2003, Pubmed
Akey,
Histone chaperones and nucleosome assembly.
2003,
Pubmed
Arents,
The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.
1991,
Pubmed
Arents,
The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization.
1995,
Pubmed
Bailey,
Both DNA and histone fold sequences contribute to archaeal nucleosome stability.
2002,
Pubmed
Banks,
Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome.
2004,
Pubmed
Banks,
Equilibrium folding of the core histones: the H3-H4 tetramer is less stable than the H2A-H2B dimer.
2003,
Pubmed
Chantalat,
Structure of the histone-core octamer in KCl/phosphate crystals at 2.15 A resolution.
2003,
Pubmed
Davey,
Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution.
2002,
Pubmed
,
Xenbase
Decanniere,
Crystal structures of recombinant histones HMfA and HMfB from the hyperthermophilic archaeon Methanothermus fervidus.
2000,
Pubmed
,
Xenbase
Decanniere,
Crystallization and preliminary X-ray characterization of the Methanothermus fervidus histones HMfA and HMfB.
1996,
Pubmed
Gloss,
The effect of salts on the stability of the H2A-H2B histone dimer.
2002,
Pubmed
,
Xenbase
Grayling,
Structure and stability of histone HMf from the hyperthermophilic archaeon Methanothermus fervidus.
1995,
Pubmed
Grayling,
DNA stability and DNA binding proteins.
1996,
Pubmed
Harp,
Asymmetries in the nucleosome core particle at 2.5 A resolution.
2000,
Pubmed
Karantza,
Thermodynamic studies of the core histones: pH and ionic strength effects on the stability of the (H3-H4)/(H3-H4)2 system.
1996,
Pubmed
Karantza,
Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability.
1995,
Pubmed
Luger,
Crystal structure of the nucleosome core particle at 2.8 A resolution.
1997,
Pubmed
Park,
Energy functions that discriminate X-ray and near native folds from well-constructed decoys.
1996,
Pubmed
Pereira,
Histones and nucleosomes in Archaea and Eukarya: a comparative analysis.
1998,
Pubmed
Placek,
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
2002,
Pubmed
,
Xenbase
Reeve,
Archaeal histones: structures, stability and DNA binding.
2004,
Pubmed
Rose,
Hydrophobic basis of packing in globular proteins.
1980,
Pubmed
Shindyalov,
Protein structure alignment by incremental combinatorial extension (CE) of the optimal path.
1998,
Pubmed
Silverman,
Hydrophobic moments of tertiary protein structures.
2003,
Pubmed
Silverman,
Hydrophobic moments of protein structures: spatially profiling the distribution.
2001,
Pubmed
Soares,
Conserved eukaryotic histone-fold residues substituted into an archaeal histone increase DNA affinity but reduce complex flexibility.
2003,
Pubmed
White,
Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions.
2001,
Pubmed
,
Xenbase
Zhou,
Spatial profiling of protein hydrophobicity: native vs. decoy structures.
2003,
Pubmed
