ArticleThe Journal of biological chemistry2010
Individual lysine acetylations on the N terminus of Saccharomyces cerevisiae H2A.Z are highly but not differentially regulated.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- DEAD-box ATPase Dbp2 is the key enzyme in an mRNP assembly checkpoint at the 3'-end of genes and involved in the recycling of cleavage factors.Nature communications · 2024Article
- Loss of TIP60 (KAT5) abolishes H2AZ lysine 7 acetylation and causes p53, INK4A, and ARF-independent cell cycle arrest.Cell death & disease · 2022Article
- The Role of the Histone Variant H2A.Z in Metazoan Development.Journal of developmental biology · 2022Review
- Ten decadal advances in fungal biology leading towards human well-being.Fungal diversity · 2022Review
- Tip60 activates Hoxa9 and Meis1 expression through acetylation of H2A.Z, promoting MLL-AF10 and MLL-ENL acute myeloid leukemia.Leukemia · 2021Article
- Insights Into the Function of the NuA4 Complex in Plants.Frontiers in plant science · 2020Review
- The histone variant H2A.Z in gene regulation.Epigenetics & chromatin · 2019Review
- Article
- Histone variants and epigenetics.Cold Spring Harbor perspectives in biology · 2015Review
- H2A.Z: a molecular rheostat for transcriptional control.F1000prime reports · 2015Review
- Catalysis-dependent stabilization of Bre1 fine-tunes histone H2B ubiquitylation to regulate gene transcription.Genes & development · 2014Article
- Identification of a BET family bromodomain/casein kinase II/TAF-containing complex as a regulator of mitotic condensin function.Cell reports · 2014Article
- Post-translational modifications of the histone variant H2AZ.Stem cell research · 2014Review
- High-resolution network biology: connecting sequence with function.Nature reviews. Genetics · 2013Review
- Histone variant Htz1 promotes histone H3 acetylation to enhance nucleotide excision repair in Htz1 nucleosomes.Nucleic acids research · 2013Article
- Histone variant H2A.Z functions in sister chromatid cohesion in Saccharomyces cerevisiae.Molecular and cellular biology · 2013Article
- Mutations in non-acid patch residues disrupt H2A.Z's association with chromatin through multiple mechanisms.PloS one · 2013Article
- The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106 co-operate to maintain promoter fidelity.The Journal of biological chemistry · 2012Article
- Revealing histone variant induced changes via quantitative proteomics.Critical reviews in biochemistry and molecular biology · 2011Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The multi-functional histone variant Htz1 (Saccharomyces cerevisiae H2A.Z) is acetylated on up to four N-terminal lysines at positions 3, 8, 10, and 14. It has thus been posited that specific acetylated forms of the histone could regulate distinct roles. Antibodies against Htz1-K8(Ac), -K10(Ac), and -K14(Ac) show that all three modifications are added by Esa1 acetyltransferase and removed by Hda1 deacetylase. Completely unacetylatable htz1 alleles exhibit widespread interactions in genome scale genetic screening. However, singly mutated (e.g. htz1-K8R) or singly acetylable (e.g. the triple mutant htz1-K3R/K10R/K14R) alleles show no significant defects in these analyses. This suggests that the N-terminal acetylations on Htz1 are internally redundant. Further supporting this proposal, each acetylation decays with similar kinetics when Htz1 transcription is repressed, and proteomic screening did not find a single condition in which one Htz1(Ac) was differentially regulated. However, whereas the individual acetylations on Htz1 may be redundant, they are not dispensable. Completely unacetylatable htz1 alleles display genetic interactions and phenotypes in common with and distinct from htz1Δ. In addition, each Htz1 N-terminal lysine is deacetylated by Hda1 in response to benomyl and reacetylated when this agent is removed. Such active regulation suggests that acetylation plays a significant role in Htz1 function.
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Registered trials
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