| What makes a histone variant a variant: Changing H2A to become H2A.Z. | What makes a histone variant a variant: Changing H2A to become H2A.Z.
Brewis HT, Wang AY, Gaub A, Lau JJ, Stirling PC, Kobor MS., Free PMC Article | 02/19/2022 |
| Influence of sequence length and charged residues on Swc5 binding with histone H2A-H2B. | Influence of sequence length and charged residues on Swc5 binding with histone H2A-H2B.
Chu WT, Wang J. | 09/11/2021 |
| H2A.1 promotes high-fidelity homologous recombination, sister chromatid recombination (SCR), and break-induced replication whereas H2A.2 does not share these functions. Both decreased SCR and the increase in CAG expansions were due to the unique Thr126 residue in H2A.1 and hta1Delta or hta1-T126A mutants were epistatic to deletion of the Poldelta subunit Pol32, suggesting a role for H2A.1 in D-loop extension. | Distinct roles for S. cerevisiae H2A copies in recombination and repeat stability, with a role for H2A.1 threonine 126.
House NC, Polleys EJ, Quasem I, De la Rosa Mejia M, Joyce CE, Takacsi-Nagy O, Krebs JE, Fuchs SM, Freudenreich CH., Free PMC Article | 05/30/2020 |
| The article identifies proteins that directly bind the acidic patch in Saccharomyces cerevisiae: histone H2A binds to Paf1 complex subunit Rtf1 and FACT subunit Spt16. | The nucleosome acidic patch directly interacts with subunits of the Paf1 and FACT complexes and controls chromatin architecture in vivo.
Cucinotta CE, Hildreth AE, McShane BM, Shirra MK, Arndt KM., Free PMC Article | 12/14/2019 |
| This study not only demonstrates the applications of the versatile histone library, but also reveals many previously unknown functions of histone H2A and H2B. | Dissecting Nucleosome Function with a Comprehensive Histone H2A and H2B Mutant Library.
Jiang S, Liu Y, Xu C, Wang Y, Gong J, Shen Y, Wu Q, Boeke JD, Dai J., Free PMC Article | 07/21/2018 |
| Robust preinitiation complex-dependent H2A.Z eviction was observed at active and infrequently transcribed genes, indicating that constitutive H2A.Z turnover is a general phenomenon. | Constitutive turnover of histone H2A.Z at yeast promoters requires the preinitiation complex.
Tramantano M, Sun L, Au C, Labuz D, Liu Z, Chou M, Shen C, Luk E., Free PMC Article | 12/2/2017 |
| Dual function of Swc5 in SWR remodeling ATPase activation and histone H2A eviction has been reported. | Dual function of Swc5 in SWR remodeling ATPase activation and histone H2A eviction.
Sun L, Luk E., Free PMC Article | 10/21/2017 |
| Data indicate that copy number variation (CNV) is regulated by both promoter activity and acetylation of histone H3 lysine 56 (H3K56ac) and that H3K56ac is required for copper-resistance gene CUP1 CNV and efficient copper adaptation. | Environmental change drives accelerated adaptation through stimulated copy number variation.
Hull RM, Cruz C, Jack CV, Houseley J., Free PMC Article | 10/7/2017 |
| A Nap1 dimer provides an acidic binding surface and asymmetrically engages a single H2A-H2B heterodimer. | Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.
Aguilar-Gurrieri C, Larabi A, Vinayachandran V, Patel NA, Yen K, Reja R, Ebong IO, Schoehn G, Robinson CV, Pugh BF, Panne D., Free PMC Article | 07/1/2017 |
| Nap1 is essential for maintaining proper chromatin composition and modulating the exchange of H2A-H2B in vivo. | Histone Chaperone Nap1 Is a Major Regulator of Histone H2A-H2B Dynamics at the Inducible GAL Locus.
Chen X, D'Arcy S, Radebaugh CA, Krzizike DD, Giebler HA, Huang L, Nyborg JK, Luger K, Stargell LA., Free PMC Article | 09/17/2016 |
| The authors found that SWR1 primarily recognizes key residues within the alpha2 helix in the histone-fold of nucleosomal histone H2A, a region not previously known to influence remodeler activity. | H2A histone-fold and DNA elements in nucleosome activate SWR1-mediated H2A.Z replacement in budding yeast.
Ranjan A, Wang F, Mizuguchi G, Wei D, Huang Y, Wu C., Free PMC Article | 04/9/2016 |
| FACT, a heterodimer of Spt16 and Pob3, disrupts nucleosome structure by binding H2A-H2B with conserved peptide motifs. | FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs.
Kemble DJ, McCullough LL, Whitby FG, Formosa T, Hill CP., Free PMC Article | 01/30/2016 |
| histone H2A Ser122 facilitates DNA repair | Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair.
Harvey AC, Jackson SP, Downs JA., Free PMC Article | 01/21/2010 |