ArticleMolecular genetics and genomics : MGG2011
Histone H2A.Z acid patch residues required for deposition and function.
Article in Molecular genetics and genomics : MGG, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024Review
- What makes a histone variant a variant: Changing H2A to become H2A.Z.PLoS genetics · 2021Article
- MacroH2A1 chromatin specification requires its docking domain and acetylation of H2B lysine 20.Nature communications · 2018Article
- Genome-wide identification of histone H2A and histone variant H2A.Z-interacting proteins by bPPI-seq.Cell research · 2017Article
- Redundant Functions for Nap1 and Chz1 in H2A.Z Deposition.Scientific reports · 2017Article
- Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1.Nature structural & molecular biology · 2016Article
- Article
- Mutations in non-acid patch residues disrupt H2A.Z's association with chromatin through multiple mechanisms.PloS one · 2013Article
- H2A.Z acidic patch couples chromatin dynamics to regulation of gene expression programs during ESC differentiation.PLoS genetics · 2013Article
- Histone H2A variants in nucleosomes and chromatin: more or less stable?Nucleic acids research · 2012Review
- Ascending the nucleosome face: recognition and function of structured domains in the histone H2A-H2B dimer.Biochimica et biophysica acta · 2012Article
- H2A.Z.2.2 is an alternatively spliced histone H2A.Z variant that causes severe nucleosome destabilization.Nucleic acids research · 2012Article
- A conserved function for the H2A.Z C terminus.The Journal of biological chemistry · 2012Article
- Key functional regions in the histone variant H2A.Z C-terminal docking domain.Molecular and cellular biology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The incorporation of histone variants is one mechanism used by the eukaryotic cell to alter the generally repressive chromatin template. However, the exact molecular mechanisms that direct this incorporation are not well understood. The SWR1 chromatin remodeling complex that binds to and directs incorporation of histone variant H2A.Z into chromatin has been characterized, but significantly less information is available concerning the requirements on the H2A.Z target molecule. We performed an unbiased mutagenic screen designed to elucidate the function of H2A.Z in Saccharomyces cerevisiae. The screen identified residues within the conserved acidic patch of H2A.Z as being important for the function of the variant. We characterized single point mutations in the patch that are phenotypically sensitive to a variety of growth conditions and are expressed at lower protein levels, but are functionally defective (htz1-D99A, htz1-D99K, and htz1-E101K). The mutants were significantly less detectable by chromatin immunoprecipitation at PHO5, a gene previously described to be enriched for H2A.Z. These results identify acidic patch residues of H2A.Z that are critical for mediating deposition and function in chromatin, and represent potential candidates for the interaction of H2A.Z with its deposition and/or targeting machinery.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.