Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 subcomplex

Alqarni, Saad S. M., Murthy, Andal, Zhang, Wei, Przewloka, Marcin R., Silva, Ana P. G., Watson, Aleksandra A., Lejon, Sara, Pei, Xue Y., Smits, Arne H., Kloet, Susan L., Wang, Hongxin, Shepherd, Nicholas E., Stokes, Philippa H., Blobel, Gerd A., Vermeulen, Michiel, Glover, David M., Mackay, Joel P. and Laue, Ernest D. (2014) Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 subcomplex. Journal of Biological Chemistry, 289 32: 21844-21855. doi:10.1074/jbc.M114.558940

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Author Alqarni, Saad S. M.
Murthy, Andal
Zhang, Wei
Przewloka, Marcin R.
Silva, Ana P. G.
Watson, Aleksandra A.
Lejon, Sara
Pei, Xue Y.
Smits, Arne H.
Kloet, Susan L.
Wang, Hongxin
Shepherd, Nicholas E.
Stokes, Philippa H.
Blobel, Gerd A.
Vermeulen, Michiel
Glover, David M.
Mackay, Joel P.
Laue, Ernest D.
Title Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 subcomplex
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 1083-351X
Publication date 2014-08-08
Year available 2014
Sub-type Article (original research)
DOI 10.1074/jbc.M114.558940
Open Access Status File (Publisher version)
Volume 289
Issue 32
Start page 21844
End page 21855
Total pages 12
Place of publication Rockville, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
The nucleosome remodeling and deacetylase (NuRD) complex is a widely conserved transcriptional co-regulator that harbors both nucleosome remodeling and histone deacetylase activities. It plays a critical role in the early stages of ES cell differentiation and the reprogramming of somatic to induced pluripotent stem cells. Abnormalities in several NuRD proteins are associated with cancer and aging. We have investigated the architecture of NuRD by determining the structure of a subcomplex comprising RbAp48 and MTA1. Surprisingly, RbAp48 recognizes MTA1 using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46/48 interactions with histones. Taken together with other results, our data show that the MTA proteins act as scaffolds for NuRD complex assembly. We further show that the RbAp48-MTA1 interaction is essential for the in vivo integration of RbAp46/48 into the NuRD complex.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 21 times in Thomson Reuters Web of Science Article | Citations
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