The MTA1 subunit of the nucleosome remodeling and deacetylase complex can recruit two copies of RBBP4/7

Schmidberger, Jason W., Sharifi Tabar, Mehdi, Torrado, Mario, Silva, Ana P. G., Landsberg, Michael J., Brillault, Lou, AlQarni, Saad, Zeng, Yi Cheng, Parker, Benjamin L., Low, Jason K. K. and Mackay, Joel P. (2016) The MTA1 subunit of the nucleosome remodeling and deacetylase complex can recruit two copies of RBBP4/7. Protein Science, 25 8: 1472-1482. doi:10.1002/pro.2943


Author Schmidberger, Jason W.
Sharifi Tabar, Mehdi
Torrado, Mario
Silva, Ana P. G.
Landsberg, Michael J.
Brillault, Lou
AlQarni, Saad
Zeng, Yi Cheng
Parker, Benjamin L.
Low, Jason K. K.
Mackay, Joel P.
Title The MTA1 subunit of the nucleosome remodeling and deacetylase complex can recruit two copies of RBBP4/7
Journal name Protein Science   Check publisher's open access policy
ISSN 0961-8368
1469-896X
Publication date 2016-05-04
Sub-type Article (original research)
DOI 10.1002/pro.2943
Open Access Status Not Open Access
Volume 25
Issue 8
Start page 1472
End page 1482
Total pages 11
Place of publication Hoboken, NJ, United States
Publisher Wiley-Blackwell
Collection year 2017
Language eng
Formatted abstract
The nucleosome remodeling and deacetylase (NuRD) complex remodels the genome in the context of both gene transcription and DNA damage repair. It is essential for normal development and is distributed across multiple tissues in organisms ranging from mammals to nematode worms. In common with other chromatin-remodeling complexes, however, its molecular mechanism of action is not well understood and only limited structural information is available to show how the complex is assembled. As a step towards understanding the structure of the NuRD complex, we have characterized the interaction between two subunits: the metastasis associated protein MTA1 and the histone-binding protein RBBP4. We show that MTA1 can bind to two molecules of RBBP4 and present negative stain electron microscopy and chemical crosslinking data that allow us to build a low-resolution model of an MTA1-(RBBP4)2 subcomplex. These data build on our understanding of NuRD complex structure and move us closer towards an understanding of the biochemical basis for the activity of this complex.
Keyword Chromatin
MTA1
NuRD complex
Protein structure
RBBP4
Transcription regulation
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 06 May 2016, 11:40:43 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences