ArticleMolecular and cellular biology2007
Contribution of the serine 129 of histone H2A to chromatin structure.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
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- Mechanism of auto-inhibition and activation of Mec1Nature structural & molecular biology · 2021Article
- Review
- DNA damage and gene transcription: accident or necessity?Cell research · 2015Article
- Heterochromatin formation via recruitment of DNA repair proteins.Molecular biology of the cell · 2015Article
- Multiple facets of histone variant H2AX: a DNA double-strand-break marker with several biological functions.Nucleic acids research · 2015Review
- Phenothiazine Inhibitors of TLKs Affect Double-Strand Break Repair and DNA Damage Response Recovery and Potentiate Tumor Killing with Radiomimetic Therapy.Genes & cancer · 2013Article
- Histone H2A variants in nucleosomes and chromatin: more or less stable?Nucleic acids research · 2012Review
- Implication of posttranslational histone modifications in nucleotide excision repair.International journal of molecular sciences · 2012Review
- A peek into the complex realm of histone phosphorylation.Molecular and cellular biology · 2011Review
- Contributions of histone H3 nucleosome core surface mutations to chromatin structures, silencing and DNA repair.PloS one · 2011Article
- Histone H2A C-terminus regulates chromatin dynamics, remodeling, and histone H1 binding.PLoS genetics · 2010Article
- Epigenetic modifications in double-strand break DNA damage signaling and repair.Clinical cancer research : an official journal of the American Association for Cancer Research · 2010Review
- Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding.The Journal of biological chemistry · 2010Article
- Epigenome manipulation as a pathway to new natural product scaffolds and their congeners.Natural product reports · 2010Review
- Dissection of Rad9 BRCT domain function in the mitotic checkpoint response to telomere uncapping.DNA repair · 2009Article
- A new paradigm for MAPK: structural interactions of hERK1 with mitochondria in HeLa cells.PloS one · 2009Article
- Inhibition of transcription at radiation-induced nuclear foci of phosphorylated histone H2AX in mammalian cells.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation of a yeast histone H2A at C-terminal serine 129 has a central role in double-strand break repair. Mimicking H2A phosphorylation by replacement of serine 129 with glutamic acid (hta1-S129E) suggested that phosphorylation destabilizes chromatin structures and thereby facilitates the access of repair proteins. Here we have tested chromatin structures in hta1-S129 mutants and in a C-terminal tail deletion strain. We show that hta1-S129E affects neither nucleosome positioning in minichromosomes and genomic loci nor supercoiling of minichromosomes. Moreover, hta1-S129E has no effect on chromatin stability measured by conventional nuclease digestion, nor does it affect DNA accessibility and repair of UV-induced DNA lesions by nucleotide excision repair and photolyase in vivo. Similarly, deletion of the C-terminal tail has no effect on nucleosome positioning and stability. These data argue against a general role for the C-terminal tail in chromatin organization and suggest that phosphorylated H2A, gamma-H2AX in higher eukaryotes, acts by recruitment of repair components rather than by destabilizing chromatin structures.
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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.