Dataset Information

Structure Change from ?-Strand and Turn to ?-Helix in Histone H2A-H2B Induced by DNA Damage Response.

ABSTRACT: Using synchrotron radiation-based circular dichroism spectroscopy, we found that the DNA damage response induces an increase of ?-helix structure and a decrease of ?-strand and turn structures in histone H2A-H2B extracted from x-irradiated human HeLa cells. The structural alterations correspond to the assumption that an average of eight amino acid residues form new ?-helix structures at 310 K. We propose the structural transition from ?-strand and turn structures to an ?-helix structure in H2A-H2B as a novel, to our knowledge, process involved in the DNA damage response.

SUBMITTER: Izumi Y

PROVIDER: S-EPMC4945303 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature

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Publications

Structure Change from β-Strand and Turn to α-Helix in Histone H2A-H2B Induced by DNA Damage Response.

Izumi Yudai Y Fujii Kentaro K Wien Frank F Houée-Lévin Chantal C Lacombe Sandrine S Salado-Leza Daniela D Porcel Erika E Masoud Rawand R Yamamoto Satoshi S Réfrégiers Matthieu M Hervé du Penhoat Marie-Anne MA Yokoya Akinari A

Biophysical journal 20160701 1

Using synchrotron radiation-based circular dichroism spectroscopy, we found that the DNA damage response induces an increase of α-helix structure and a decrease of β-strand and turn structures in histone H2A-H2B extracted from x-irradiated human HeLa cells. The structural alterations correspond to the assumption that an average of eight amino acid residues form new α-helix structures at 310 K. We propose the structural transition from β-strand and turn structures to an α-helix structure in H2A-H ...[more]

PMID: 27410735

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Project description:In Saccharomyces cerevisiae, a single double-strand break (DSB) triggers extensive phosphorylation of histone H2A (known as gammaH2AX) over 50 kb on either side of the DSB. This modification is carried out by either of yeastM-^Rs checkpoint kinases, the ATM homolog, Tel1, or the ATR homolog, Mec1. In G1-arrested cells, where there is very little 5M-^R to 3M-^R processing of DSB ends, only Tel1 promotes this modification. We have recently described a second modification gammaH2B - the phosphorylation of the C terminal T129 locus of histone H2B which is also carried out by both Mec1 and Tel1 kinases. To understand in detail how gamma-H2AX and gamma-H2B spread along the chromosome from a DSB we have undertaken a high-density analysis of their occupancy where there is a DSB on three different chromosomes. gamma-H2AX and gamma-H2B modifications are similar, but there is a marked absence of gamma-H2B near telomeres. We find that there is reduced gamma-H2AX and gamma-H2B modification over strongly transcribed regions, even taking into account the reduced histone occupancy of these genes. When transcription of the galactose-regulated genes GAL1, GAL10, GAL7 are turned off by the addition of glucose, gamma-H2AX is restored within 5 min; when these genes are again induced, gamma-H2AX is rapidly lost. Regions more distal to the GAL genes have markedly reduced gamma-H2AX levels that rise rapidly when transcription is repressed, suggesting that transcription acts as a barrier to the propagation of gamma-H2AX away from the DSB. The restoration of gamma-H2AX in transcribed regions can be carried out by either Mec1 or Tel1, even 7 h after break induction, suggesting that Tel1 remains associated with damaged chromosomes for an extended time. In addition, we show that gamma-H2AX can be transferred in trans, to regions unlinked to the DSB that lie in close proximity the DSB. Specifically, if a DSB is generated 14 kb from CEN2, gamma-H2AX is transferred to regions around all the other centromeres, in keeping with observed close proximity of all centromere-adjacent chromosome arms. This transfer can be observed even in the absence of formaldehyde crosslinking of the samples.

Dataset Information

Structure Change from ?-Strand and Turn to ?-Helix in Histone H2A-H2B Induced by DNA Damage Response.

Publications

Structure Change from β-Strand and Turn to α-Helix in Histone H2A-H2B Induced by DNA Damage Response.

Similar Datasets

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