CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex

Cornelia G. Spruijt; Stefanie J.J. Bartels; Arie B. Brinkman; Jorrit V. Tjeertes; Ina Poser; Hendrik G. Stunnenberg; Michiel Vermeulen

doi:10.1039/c004108d

CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex

Cornelia G. Spruijt
, Stefanie J.J. Bartels
, Arie B. Brinkman
, Jorrit V. Tjeertes
, Ina Poser
, Hendrik G. Stunnenberg
, Michiel Vermeulen

Research output: Contribution to journal › Article › peer-review

48 Citations (Scopus)

Abstract

The Mi-2/NuRD (NUcleosome Remodeling and histone Deacetylase) chromatin remodeling complex is a large heterogeneous multiprotein complex associated with transcriptional repression. Here we apply a SILAC based quantitative proteomics approach to show that all known Mi-2/NuRD complex subunits co-purify with Cyclin Dependent Kinase 2 Associated Protein1 (CDK2AP1), also known as Deleted in Oral Cancer 1 (DOC-1). DOC-1 displays in vitro binding affinity for methylated DNA as part of the meCpG binding MBD2/NuRD complex. In luciferase reporter assays, DOC-1 is a potent repressor of transcription. Finally, immunofluorescence experiments reveal co-localization between MBD2 and DOC-1 in mouse NIH-3T3 nuclei. Collectively, these results indicate that DOC-1 is a bona fide subunit of the Mi-2/NuRD chromatin remodeling complex.

Original language	English
Pages (from-to)	1700-1706
Number of pages	7
Journal	Molecular BioSystems
Volume	6
Issue number	9
DOIs	https://doi.org/10.1039/c004108d
Publication status	Published - Sept 2010
Externally published	Yes

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title = "CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex",

abstract = "The Mi-2/NuRD (NUcleosome Remodeling and histone Deacetylase) chromatin remodeling complex is a large heterogeneous multiprotein complex associated with transcriptional repression. Here we apply a SILAC based quantitative proteomics approach to show that all known Mi-2/NuRD complex subunits co-purify with Cyclin Dependent Kinase 2 Associated Protein1 (CDK2AP1), also known as Deleted in Oral Cancer 1 (DOC-1). DOC-1 displays in vitro binding affinity for methylated DNA as part of the meCpG binding MBD2/NuRD complex. In luciferase reporter assays, DOC-1 is a potent repressor of transcription. Finally, immunofluorescence experiments reveal co-localization between MBD2 and DOC-1 in mouse NIH-3T3 nuclei. Collectively, these results indicate that DOC-1 is a bona fide subunit of the Mi-2/NuRD chromatin remodeling complex.",

author = "Spruijt, \{Cornelia G.\} and Bartels, \{Stefanie J.J.\} and Brinkman, \{Arie B.\} and Tjeertes, \{Jorrit V.\} and Ina Poser and Stunnenberg, \{Hendrik G.\} and Michiel Vermeulen",

year = "2010",

month = sep,

doi = "10.1039/c004108d",

language = "English",

volume = "6",

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T1 - CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex

AU - Spruijt, Cornelia G.

AU - Bartels, Stefanie J.J.

AU - Brinkman, Arie B.

AU - Tjeertes, Jorrit V.

AU - Poser, Ina

AU - Stunnenberg, Hendrik G.

AU - Vermeulen, Michiel

PY - 2010/9

Y1 - 2010/9

N2 - The Mi-2/NuRD (NUcleosome Remodeling and histone Deacetylase) chromatin remodeling complex is a large heterogeneous multiprotein complex associated with transcriptional repression. Here we apply a SILAC based quantitative proteomics approach to show that all known Mi-2/NuRD complex subunits co-purify with Cyclin Dependent Kinase 2 Associated Protein1 (CDK2AP1), also known as Deleted in Oral Cancer 1 (DOC-1). DOC-1 displays in vitro binding affinity for methylated DNA as part of the meCpG binding MBD2/NuRD complex. In luciferase reporter assays, DOC-1 is a potent repressor of transcription. Finally, immunofluorescence experiments reveal co-localization between MBD2 and DOC-1 in mouse NIH-3T3 nuclei. Collectively, these results indicate that DOC-1 is a bona fide subunit of the Mi-2/NuRD chromatin remodeling complex.

AB - The Mi-2/NuRD (NUcleosome Remodeling and histone Deacetylase) chromatin remodeling complex is a large heterogeneous multiprotein complex associated with transcriptional repression. Here we apply a SILAC based quantitative proteomics approach to show that all known Mi-2/NuRD complex subunits co-purify with Cyclin Dependent Kinase 2 Associated Protein1 (CDK2AP1), also known as Deleted in Oral Cancer 1 (DOC-1). DOC-1 displays in vitro binding affinity for methylated DNA as part of the meCpG binding MBD2/NuRD complex. In luciferase reporter assays, DOC-1 is a potent repressor of transcription. Finally, immunofluorescence experiments reveal co-localization between MBD2 and DOC-1 in mouse NIH-3T3 nuclei. Collectively, these results indicate that DOC-1 is a bona fide subunit of the Mi-2/NuRD chromatin remodeling complex.

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EP - 1706

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CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex

Abstract

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