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A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast

The highly charged histone N-terminal domains are engaged in inter- and intra-nucleosomal interactions, and contain a host of sites used for posttranslational modification. We have studied the effect of deleting residues 30–37 from the N-terminal domain of histone H2B in yeast cells, on nucleotide e...

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Autores principales: Nag, Ronita, Kyriss, McKenna, Smerdon, John W., Wyrick, John J., Smerdon, Michael J.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2836547/
https://www.ncbi.nlm.nih.gov/pubmed/20007597
http://dx.doi.org/10.1093/nar/gkp1074
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author Nag, Ronita
Kyriss, McKenna
Smerdon, John W.
Wyrick, John J.
Smerdon, Michael J.
author_facet Nag, Ronita
Kyriss, McKenna
Smerdon, John W.
Wyrick, John J.
Smerdon, Michael J.
author_sort Nag, Ronita
collection PubMed
description The highly charged histone N-terminal domains are engaged in inter- and intra-nucleosomal interactions, and contain a host of sites used for posttranslational modification. We have studied the effect of deleting residues 30–37 from the N-terminal domain of histone H2B in yeast cells, on nucleotide excision repair (NER) following UV irradiation, as these cells are quite sensitive to UV. We find that H2B Δ30–37 cells exhibit reduced NER efficiency at three specific chromatin loci: the transcriptionally active, RPB2 locus; the transcriptionally silenced, nucleosome-loaded HML locus; and the transcriptionally repressed, non-silenced, GAL10 locus. Nuclease digestion studies indicate that H2B Δ30–37 chromatin has increased nucleosome accessibility and/or nucleosome mobility. In addition, H2B Δ30–37 mutants acquire more DNA damage, compared to wt cells, following the same dose of UV radiation. Reducing the level of damage in H2B Δ30–37 cells to match that of wt cells restores the NER rate to wt levels in the RPB2 and GAL10 loci, but NER efficiency remains low in the silenced HML locus. Interestingly, recruitment of Snf5 to the HML locus is reduced in H2B Δ30–37 cells and more transient following UV irradiation. This may reflect a lower binding affinity of the SWI/SNF complex to H2B Δ30–37 nucleosomes.
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spelling pubmed-28365472010-03-11 A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast Nag, Ronita Kyriss, McKenna Smerdon, John W. Wyrick, John J. Smerdon, Michael J. Nucleic Acids Res Genome Integrity, Repair and Replication The highly charged histone N-terminal domains are engaged in inter- and intra-nucleosomal interactions, and contain a host of sites used for posttranslational modification. We have studied the effect of deleting residues 30–37 from the N-terminal domain of histone H2B in yeast cells, on nucleotide excision repair (NER) following UV irradiation, as these cells are quite sensitive to UV. We find that H2B Δ30–37 cells exhibit reduced NER efficiency at three specific chromatin loci: the transcriptionally active, RPB2 locus; the transcriptionally silenced, nucleosome-loaded HML locus; and the transcriptionally repressed, non-silenced, GAL10 locus. Nuclease digestion studies indicate that H2B Δ30–37 chromatin has increased nucleosome accessibility and/or nucleosome mobility. In addition, H2B Δ30–37 mutants acquire more DNA damage, compared to wt cells, following the same dose of UV radiation. Reducing the level of damage in H2B Δ30–37 cells to match that of wt cells restores the NER rate to wt levels in the RPB2 and GAL10 loci, but NER efficiency remains low in the silenced HML locus. Interestingly, recruitment of Snf5 to the HML locus is reduced in H2B Δ30–37 cells and more transient following UV irradiation. This may reflect a lower binding affinity of the SWI/SNF complex to H2B Δ30–37 nucleosomes. Oxford University Press 2010-03 2009-12-09 /pmc/articles/PMC2836547/ /pubmed/20007597 http://dx.doi.org/10.1093/nar/gkp1074 Text en © The Author(s) 2009. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Genome Integrity, Repair and Replication
Nag, Ronita
Kyriss, McKenna
Smerdon, John W.
Wyrick, John J.
Smerdon, Michael J.
A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast
title A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast
title_full A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast
title_fullStr A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast
title_full_unstemmed A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast
title_short A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast
title_sort cassette of n-terminal amino acids of histone h2b are required for efficient cell survival, dna repair and swi/snf binding in uv irradiated yeast
topic Genome Integrity, Repair and Replication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2836547/
https://www.ncbi.nlm.nih.gov/pubmed/20007597
http://dx.doi.org/10.1093/nar/gkp1074
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