ArticleMolecular and cellular biology2003
The nonessential H2A N-terminal tail can function as an essential charge patch on the H2A.Z variant N-terminal tail.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- Bromodomain protein IBD1 bridges histone acetylation and H2A.Z deposition to fine-tune transcription.Nucleic acids research · 2026Article
- BPTF Target Engagement by Acetylated H2A.Z Photoaffinity Probes.Biochemistry · 2025Article
- Histone variant H2B.Z acetylation is necessary for maintenance of Toxoplasma gondii biological fitness.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Article
- Histone variant H2B.Z acetylation is necessary for maintenance ofbioRxiv : the preprint server for biology · 2023Article
- The bromodomains of BET family proteins can recognize diacetylated histone H2A.Z.Protein science : a publication of the Protein Society · 2021Article
- New roles for old modifications: emerging roles of N-terminal post-translational modifications in development and disease.Protein science : a publication of the Protein Society · 2014Review
- Histone variant H2A.Z and RNA polymerase II transcription elongation.Molecular and cellular biology · 2011Article
- Individual lysine acetylations on the N terminus of Saccharomyces cerevisiae H2A.Z are highly but not differentially regulated.The Journal of biological chemistry · 2010Article
- Overexpression of several Arabidopsis histone genes increases agrobacterium-mediated transformation and transgene expression in plants.The Plant cell · 2009Article
- Acetylation of vertebrate H2A.Z and its effect on the structure of the nucleosome.Biochemistry · 2009Article
- Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4.Molecular and cellular biology · 2009Article
- Computer modeling reveals that modifications of the histone tail charges define salt-dependent interaction of the nucleosome core particles.Biophysical journal · 2009Article
- HDAC6 modulates cell motility by altering the acetylation level of cortactin.Molecular cell · 2007Article
- Phosphorylation of the SQ H2A.X motif is required for proper meiosis and mitosis in Tetrahymena thermophila.Molecular and cellular biology · 2007Article
- Computer modeling demonstrates that electrostatic attraction of nucleosomal DNA is mediated by histone tails.Biophysical journal · 2006Article
- Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae.Genes & development · 2006Article
- Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Tetrahymena thermophila cells contain three forms of H2A: major H2A.1 and H2A.2, which make up approximately 80% of total H2A, and a conserved variant, H2A.Z. We showed previously that acetylation of H2A.Z was essential (Q. Ren and M. A. Gorovsky, Mol. Cell 7:1329-1335, 2001). Here we used in vitro mutagenesis of lysine residues, coupled with gene replacement, to identify the sites of acetylation of the N-terminal tail of the major H2A and to analyze its function in vivo. Tetrahymena cells survived with all five acetylatable lysines replaced by arginines plus a mutation that abolished acetylation of the N-terminal serine normally found in the wild-type protein. Thus, neither posttranslational nor cotranslational acetylation of major H2A is essential. Surprisingly, the nonacetylatable N-terminal tail of the major H2A was able to replace the essential function of the acetylation of the H2A.Z N-terminal tail. Tail-swapping experiments between H2A.1 and H2A.Z revealed that the nonessential acetylation of the major H2A N-terminal tail can be made to function as an essential charge patch in place of the H2A.Z N-terminal tail and that while the pattern of acetylation of an H2A N-terminal tail is determined by the tail sequence, the effects of acetylation on viability are determined by properties of the H2A core and not those of the N-terminal tail itself.
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