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The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken

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The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken. / Bruce, K.; Myers, Fiona; Mantouvalou, E.; Lefevre, P.; Greaves, I.; Bonifer, C.; Tremethick, D.; Thorne, Alan; Crane-Robinson, Colyn.

In: Nucleic Acids Research, Vol. 33, No. 17, 2005, p. 5633-5639.

Research output: Contribution to journalArticle

Harvard

Bruce, K, Myers, F, Mantouvalou, E, Lefevre, P, Greaves, I, Bonifer, C, Tremethick, D, Thorne, A & Crane-Robinson, C 2005, 'The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken', Nucleic Acids Research, vol. 33, no. 17, pp. 5633-5639. https://doi.org/10.1093/nar/gki874

APA

Bruce, K., Myers, F., Mantouvalou, E., Lefevre, P., Greaves, I., Bonifer, C., Tremethick, D., Thorne, A., & Crane-Robinson, C. (2005). The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken. Nucleic Acids Research, 33(17), 5633-5639. https://doi.org/10.1093/nar/gki874

Vancouver

Bruce K, Myers F, Mantouvalou E, Lefevre P, Greaves I, Bonifer C et al. The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken. Nucleic Acids Research. 2005;33(17):5633-5639. https://doi.org/10.1093/nar/gki874

Author

Bruce, K. ; Myers, Fiona ; Mantouvalou, E. ; Lefevre, P. ; Greaves, I. ; Bonifer, C. ; Tremethick, D. ; Thorne, Alan ; Crane-Robinson, Colyn. / The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken. In: Nucleic Acids Research. 2005 ; Vol. 33, No. 17. pp. 5633-5639.

Bibtex

@article{4b993f03dea54e4fb5bcd0fbe8d296f8,
title = "The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken",
abstract = "The replacement histone H2A.Z is variously reported as being linked to gene expression and preventing the spread of heterochromatin in yeast, or concentrated at heterochromatin in mammals. To resolve this apparent dichotomy, affinity-purified antibodies against the N-terminal region of H2A.Z, in both a triacetylated and non-acetylated state, are used in native chromatin immmuno-precipitation experiments with mononucleosomes from three chicken cell types. The hyperacetylated species concentrates at the 5′ end of active genes, both tissue specific and housekeeping but is absent from inactive genes, while the unacetylated form is absent from both active and inactive genes. A concentration of H2A.Z is also found at insulators under circumstances implying a link to barrier activity but not to enhancer blocking. Although acetylated H2A.Z is widespread throughout the interphase genome, at mitosis its acetylation is erased, the unmodified form remaining. Thus, although H2A.Z may operate as an epigenetic marker for active genes, its N-terminal acetylation does not.",
author = "K. Bruce and Fiona Myers and E. Mantouvalou and P. Lefevre and I. Greaves and C. Bonifer and D. Tremethick and Alan Thorne and Colyn Crane-Robinson",
year = "2005",
doi = "10.1093/nar/gki874",
language = "English",
volume = "33",
pages = "5633--5639",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "17",

}

RIS

TY - JOUR

T1 - The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken

AU - Bruce, K.

AU - Myers, Fiona

AU - Mantouvalou, E.

AU - Lefevre, P.

AU - Greaves, I.

AU - Bonifer, C.

AU - Tremethick, D.

AU - Thorne, Alan

AU - Crane-Robinson, Colyn

PY - 2005

Y1 - 2005

N2 - The replacement histone H2A.Z is variously reported as being linked to gene expression and preventing the spread of heterochromatin in yeast, or concentrated at heterochromatin in mammals. To resolve this apparent dichotomy, affinity-purified antibodies against the N-terminal region of H2A.Z, in both a triacetylated and non-acetylated state, are used in native chromatin immmuno-precipitation experiments with mononucleosomes from three chicken cell types. The hyperacetylated species concentrates at the 5′ end of active genes, both tissue specific and housekeeping but is absent from inactive genes, while the unacetylated form is absent from both active and inactive genes. A concentration of H2A.Z is also found at insulators under circumstances implying a link to barrier activity but not to enhancer blocking. Although acetylated H2A.Z is widespread throughout the interphase genome, at mitosis its acetylation is erased, the unmodified form remaining. Thus, although H2A.Z may operate as an epigenetic marker for active genes, its N-terminal acetylation does not.

AB - The replacement histone H2A.Z is variously reported as being linked to gene expression and preventing the spread of heterochromatin in yeast, or concentrated at heterochromatin in mammals. To resolve this apparent dichotomy, affinity-purified antibodies against the N-terminal region of H2A.Z, in both a triacetylated and non-acetylated state, are used in native chromatin immmuno-precipitation experiments with mononucleosomes from three chicken cell types. The hyperacetylated species concentrates at the 5′ end of active genes, both tissue specific and housekeeping but is absent from inactive genes, while the unacetylated form is absent from both active and inactive genes. A concentration of H2A.Z is also found at insulators under circumstances implying a link to barrier activity but not to enhancer blocking. Although acetylated H2A.Z is widespread throughout the interphase genome, at mitosis its acetylation is erased, the unmodified form remaining. Thus, although H2A.Z may operate as an epigenetic marker for active genes, its N-terminal acetylation does not.

U2 - 10.1093/nar/gki874

DO - 10.1093/nar/gki874

M3 - Article

VL - 33

SP - 5633

EP - 5639

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 17

ER -

ID: 155450