Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2

Sarah Cooper; Anne Grijzenhout; Elizabeth Underwood; Katia Ancelin; Tianyi Zhang; Tatyana B Nesterova; Burcu Anil-Kirmizitas; Andrew Bassett; Susanne M Kooistra; Karl Agger; Kristian Helin; Edith Heard; Neil Brockdorff

doi:10.1038/ncomms13661

Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2

Sarah Cooper, Anne Grijzenhout, Elizabeth Underwood, Katia Ancelin, Tianyi Zhang, Tatyana B Nesterova, Burcu Anil-Kirmizitas, Andrew Bassett, Susanne M Kooistra, Karl Agger, Kristian Helin, Edith Heard, Neil Brockdorff

108 Citationer (Scopus)

63 Downloads (Pure)

Abstract

The Polycomb repressive complexes PRC1 and PRC2 play a central role in developmental gene regulation in multicellular organisms. PRC1 and PRC2 modify chromatin by catalysing histone H2A lysine 119 ubiquitylation (H2AK119u1), and H3 lysine 27 methylation (H3K27me3), respectively. Reciprocal crosstalk between these modifications is critical for the formation of stable Polycomb domains at target gene loci. While the molecular mechanism for recognition of H3K27me3 by PRC1 is well defined, the interaction of PRC2 with H2AK119u1 is poorly understood. Here we demonstrate a critical role for the PRC2 cofactor Jarid2 in mediating the interaction of PRC2 with H2AK119u1. We identify a ubiquitin interaction motif at the amino-terminus of Jarid2, and demonstrate that this domain facilitates PRC2 localization to H2AK119u1 both in vivo and in vitro. Our findings ascribe a critical function to Jarid2 and define a key mechanism that links PRC1 and PRC2 in the establishment of Polycomb domains.

Originalsprog	Engelsk
Artikelnummer	13661
Tidsskrift	Nature Communications
Vol/bind	7
Antal sider	8
ISSN	2041-1723
DOI	https://doi.org/10.1038/ncomms13661
Status	Udgivet - 28 nov. 2016

Adgang til dokumentet

10.1038/ncomms13661Licens: CC BY

Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2Forlagets udgivne version, 1,17 MBLicens: CC BY

Citationsformater

Cooper, S., Grijzenhout, A., Underwood, E., Ancelin, K., Zhang, T., Nesterova, T. B., Anil-Kirmizitas, B., Bassett, A., Kooistra, S. M., Agger, K., Helin, K., Heard, E., & Brockdorff, N. (2016). Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2. Nature Communications, 7, [13661]. https://doi.org/10.1038/ncomms13661

@article{ade8a1b257e34d1e838037c30cfc5c54,

title = "Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2",

abstract = "The Polycomb repressive complexes PRC1 and PRC2 play a central role in developmental gene regulation in multicellular organisms. PRC1 and PRC2 modify chromatin by catalysing histone H2A lysine 119 ubiquitylation (H2AK119u1), and H3 lysine 27 methylation (H3K27me3), respectively. Reciprocal crosstalk between these modifications is critical for the formation of stable Polycomb domains at target gene loci. While the molecular mechanism for recognition of H3K27me3 by PRC1 is well defined, the interaction of PRC2 with H2AK119u1 is poorly understood. Here we demonstrate a critical role for the PRC2 cofactor Jarid2 in mediating the interaction of PRC2 with H2AK119u1. We identify a ubiquitin interaction motif at the amino-terminus of Jarid2, and demonstrate that this domain facilitates PRC2 localization to H2AK119u1 both in vivo and in vitro. Our findings ascribe a critical function to Jarid2 and define a key mechanism that links PRC1 and PRC2 in the establishment of Polycomb domains.",

author = "Sarah Cooper and Anne Grijzenhout and Elizabeth Underwood and Katia Ancelin and Tianyi Zhang and Nesterova, {Tatyana B} and Burcu Anil-Kirmizitas and Andrew Bassett and Kooistra, {Susanne M} and Karl Agger and Kristian Helin and Edith Heard and Neil Brockdorff",

year = "2016",

month = nov,

day = "28",

doi = "10.1038/ncomms13661",

language = "English",

volume = "7",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "nature publishing group",

}

TY - JOUR

T1 - Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2

AU - Cooper, Sarah

AU - Grijzenhout, Anne

AU - Underwood, Elizabeth

AU - Ancelin, Katia

AU - Zhang, Tianyi

AU - Nesterova, Tatyana B

AU - Anil-Kirmizitas, Burcu

AU - Bassett, Andrew

AU - Kooistra, Susanne M

AU - Agger, Karl

AU - Helin, Kristian

AU - Heard, Edith

AU - Brockdorff, Neil

PY - 2016/11/28

Y1 - 2016/11/28

N2 - The Polycomb repressive complexes PRC1 and PRC2 play a central role in developmental gene regulation in multicellular organisms. PRC1 and PRC2 modify chromatin by catalysing histone H2A lysine 119 ubiquitylation (H2AK119u1), and H3 lysine 27 methylation (H3K27me3), respectively. Reciprocal crosstalk between these modifications is critical for the formation of stable Polycomb domains at target gene loci. While the molecular mechanism for recognition of H3K27me3 by PRC1 is well defined, the interaction of PRC2 with H2AK119u1 is poorly understood. Here we demonstrate a critical role for the PRC2 cofactor Jarid2 in mediating the interaction of PRC2 with H2AK119u1. We identify a ubiquitin interaction motif at the amino-terminus of Jarid2, and demonstrate that this domain facilitates PRC2 localization to H2AK119u1 both in vivo and in vitro. Our findings ascribe a critical function to Jarid2 and define a key mechanism that links PRC1 and PRC2 in the establishment of Polycomb domains.

AB - The Polycomb repressive complexes PRC1 and PRC2 play a central role in developmental gene regulation in multicellular organisms. PRC1 and PRC2 modify chromatin by catalysing histone H2A lysine 119 ubiquitylation (H2AK119u1), and H3 lysine 27 methylation (H3K27me3), respectively. Reciprocal crosstalk between these modifications is critical for the formation of stable Polycomb domains at target gene loci. While the molecular mechanism for recognition of H3K27me3 by PRC1 is well defined, the interaction of PRC2 with H2AK119u1 is poorly understood. Here we demonstrate a critical role for the PRC2 cofactor Jarid2 in mediating the interaction of PRC2 with H2AK119u1. We identify a ubiquitin interaction motif at the amino-terminus of Jarid2, and demonstrate that this domain facilitates PRC2 localization to H2AK119u1 both in vivo and in vitro. Our findings ascribe a critical function to Jarid2 and define a key mechanism that links PRC1 and PRC2 in the establishment of Polycomb domains.

U2 - 10.1038/ncomms13661

DO - 10.1038/ncomms13661

M3 - Journal article

C2 - 27892467

SN - 2041-1723

VL - 7

JO - Nature Communications

JF - Nature Communications

M1 - 13661

ER -

Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2

Abstract

Adgang til dokumentet

Fingeraftryk

Citationsformater