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.
Protein Sci
2011 Dec 01;2012:2060-73. doi: 10.1002/pro.743.
Show Gene links
Show Anatomy links
The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones.
Topping TB
,
Gloss LM
.
???displayArticle.abstract???
The goal of this study was to examine fibril formation by the heterodimeric eukaryotic histones (H2A-H2B and H3-H4) and homodimeric archaeal histones (hMfB and hPyA1). The histone fold dimerization motif is an obligatorily domain-swapped structure comprised of two fused helix:β-loop:helix motifs. Domain swapping has been proposed as a mechanism for the evolution of protein oligomers as well as a means to form precursors in the formation of amyloid-like fibrils. Despite sharing a common fold, the eukaryotic histones of the core nucleosome and archaeal histones fold by kinetic mechanisms of differing complexity with transient population of partially folded monomeric and/or dimeric species. No relationship was apparent between fibrillation propensity and equilibrium stability or population of kinetic intermediates. Only H3 and H4, as isolated monomers and as a heterodimer, readily formed fibrils at room temperature, and this propensity correlates with the significantly lower solubility of these polypeptides. The fibrils were characterized by ThT fluorescence, FTIR, and far-UV CD spectroscopies and electron microscopy. The helical histone fold comprises the protease-resistant core of the fibrils, with little or no protease protection of the poorly structured N-terminal tails. The highly charged tails inhibit fibrillation through electrostatic repulsion. Kinetic studies indicate that H3 and H4 form a co-fibril, with simultaneous incorporation of both histones. The potential impact of H3 and H4 fibrillation on the cytotoxicity of extracellular histones and α-synuclein-mediated neurotoxicity and fibrillation is considered.
Abedini,
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
2009, Pubmed
Abedini,
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
2009,
Pubmed
Alva,
On the origin of the histone fold.
2007,
Pubmed
Arents,
Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA.
1993,
Pubmed
Aso,
Systematic analysis of aggregates from 38 kinds of non disease-related proteins: identifying the intrinsic propensity of polypeptides to form amyloid fibrils.
2007,
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
Baxevanis,
A variety of DNA-binding and multimeric proteins contain the histone fold motif.
1995,
Pubmed
Bennett,
3D domain swapping: a mechanism for oligomer assembly.
1995,
Pubmed
Bennett,
Deposition diseases and 3D domain swapping.
2006,
Pubmed
Berger,
The complex language of chromatin regulation during transcription.
2007,
Pubmed
Biancalana,
Molecular mechanism of Thioflavin-T binding to amyloid fibrils.
2010,
Pubmed
Birck,
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family.
1998,
Pubmed
Brinkmann,
Neutrophil extracellular traps kill bacteria.
2004,
Pubmed
Chi,
Covalent histone modifications--miswritten, misinterpreted and mis-erased in human cancers.
2010,
Pubmed
Chiti,
Amyloid formation by globular proteins under native conditions.
2009,
Pubmed
Chiti,
Rationalization of the effects of mutations on peptide and protein aggregation rates.
2003,
Pubmed
Cordeiro,
Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.
2006,
Pubmed
Davey,
Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution.
2002,
Pubmed
,
Xenbase
Eakin,
Oligomeric assembly of native-like precursors precedes amyloid formation by beta-2 microglobulin.
2004,
Pubmed
Eisenberg,
The structural biology of protein aggregation diseases: Fundamental questions and some answers.
2006,
Pubmed
Fernandez-Escamilla,
Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins.
2004,
Pubmed
Gloss,
The effect of salts on the stability of the H2A-H2B histone dimer.
2002,
Pubmed
,
Xenbase
Goers,
Nuclear localization of alpha-synuclein and its interaction with histones.
2003,
Pubmed
Goldschmidt,
Identifying the amylome, proteins capable of forming amyloid-like fibrils.
2010,
Pubmed
Gonias,
Precipitation of fibrinogen, fibrinogen degradation products and fibrin monomer by histone H3.
1985,
Pubmed
Guo,
Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I.
2006,
Pubmed
Hafner-Bratkovic,
Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion.
2011,
Pubmed
Hoyer,
Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro.
2004,
Pubmed
Janowski,
3D domain-swapped human cystatin C with amyloidlike intermolecular beta-sheets.
2005,
Pubmed
Jenko Kokalj,
Essential role of proline isomerization in stefin B tetramer formation.
2007,
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
Kenig,
Folding and amyloid-fibril formation for a series of human stefins' chimeras: any correlation?
2006,
Pubmed
Knaus,
Crystal structure of the human prion protein reveals a mechanism for oligomerization.
2001,
Pubmed
Kontopoulos,
Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity.
2006,
Pubmed
Krebs,
Observation of sequence specificity in the seeding of protein amyloid fibrils.
2004,
Pubmed
Kusumoto,
Temperature dependence of amyloid beta-protein fibrillization.
1998,
Pubmed
Lawson,
E. coli trp repressor forms a domain-swapped array in aqueous alcohol.
2004,
Pubmed
Li,
Thermodynamic stability of archaeal histones.
1998,
Pubmed
Lindgren,
Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states.
2010,
Pubmed
Liu,
3D domain swapping: as domains continue to swap.
2002,
Pubmed
Liu,
β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
2011,
Pubmed
Luger,
Crystal structure of the nucleosome core particle at 2.8 A resolution.
1997,
Pubmed
Luheshi,
Bridging the gap: from protein misfolding to protein misfolding diseases.
2009,
Pubmed
Marshall,
Hydrophobic, aromatic, and electrostatic interactions play a central role in amyloid fibril formation and stability.
2011,
Pubmed
Maurer-Stroh,
Exploring the sequence determinants of amyloid structure using position-specific scoring matrices.
2010,
Pubmed
Munishkina,
Conformational prerequisites for formation of amyloid fibrils from histones.
2004,
Pubmed
Munishkina,
Guiding protein aggregation with macromolecular crowding.
2008,
Pubmed
Newcomer,
Protein folding and three-dimensional domain swapping: a strained relationship?
2002,
Pubmed
Nilsson,
Techniques to study amyloid fibril formation in vitro.
2004,
Pubmed
Ogihara,
Design of three-dimensional domain-swapped dimers and fibrous oligomers.
2001,
Pubmed
Pace,
Protein structure, stability and solubility in water and other solvents.
2004,
Pubmed
Pemberton,
Proteomic identification of interactions between histones and plasma proteins: implications for cytoprotection.
2010,
Pubmed
Pfefferkorn,
Effects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17.
2010,
Pubmed
Picotti,
Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis.
2007,
Pubmed
Placek,
Three-state kinetic folding mechanism of the H2A/H2B histone heterodimer: the N-terminal tails affect the transition state between a dimeric intermediate and the native dimer.
2005,
Pubmed
Raman,
Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability.
2005,
Pubmed
Rousseau,
The unfolding story of three-dimensional domain swapping.
2003,
Pubmed
Sambashivan,
Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.
2005,
Pubmed
Schmittschmitt,
The role of protein stability, solubility, and net charge in amyloid fibril formation.
2003,
Pubmed
Schägger,
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.
1987,
Pubmed
Selleck,
A histone fold TAF octamer within the yeast TFIID transcriptional coactivator.
2001,
Pubmed
Stewart,
Aggregation of fibrinogen and its degradation products by basic proteins. An electron microscope study.
1971,
Pubmed
Strahl,
The language of covalent histone modifications.
2000,
Pubmed
Stump,
Mutational analysis of the stability of the H2A and H2B histone monomers.
2008,
Pubmed
Stump,
Mutational studies uncover non-native structure in the dimeric kinetic intermediate of the H2A-H2B heterodimer.
2010,
Pubmed
Sullivan,
Characterization of sequence variability in nucleosome core histone folds.
2003,
Pubmed
Takehara,
Refolding and polymerization pathways of neuroserpin.
2010,
Pubmed
Tartaglia,
The Zyggregator method for predicting protein aggregation propensities.
2008,
Pubmed
Tartaglia,
Prediction of aggregation-prone regions in structured proteins.
2008,
Pubmed
Topping,
Stability and folding mechanism of mesophilic, thermophilic and hyperthermophilic archael histones: the importance of folding intermediates.
2004,
Pubmed
Trevino,
Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa.
2007,
Pubmed
Trevino,
Measuring and increasing protein solubility.
2008,
Pubmed
Uversky,
Evidence for a partially folded intermediate in alpha-synuclein fibril formation.
2001,
Pubmed
Ventura,
Sequence determinants of protein aggregation: tools to increase protein solubility.
2005,
Pubmed
Wachtel,
Low resolution models of self-assembled histone fibers from X-ray diffraction studies.
1979,
Pubmed
Wahlbom,
Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.
2007,
Pubmed
Xie,
Structural similarity between TAFs and the heterotetrameric core of the histone octamer.
1996,
Pubmed
Xu,
Extracellular histones are major mediators of death in sepsis.
2009,
Pubmed
Žerovnik,
Mechanisms of amyloid fibril formation--focus on domain-swapping.
2011,
Pubmed
