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Reply to “Testing for association between MeCP2 and the brahma-associated SWI/SNF chromatin-remodeling complex”

Nature Genetics volume 38, pages 964–967 (2006)Cite this article

Harikrishnan et al. reply:

The arguments of Hu et al. are logically flawed and their findings inconsistent within their own work and in comparison with the work of others. Bird et al. originally published that HeLa cells lack endogenous MeCP2 (ref. 1), yet the authors purposefully draw on this cell type to support their current claims. We are critical of the suitability of this experimentation and therefore have reinvestigated these associations more closely. We repeated these experiments using four independent methods and five separate cell types to demonstrate clear and stable association between the SWI/SNF chromatin-remodeling complex containing Brahma with MeCP2 (ref. 2). The choice of HeLaS3 and other experiments by Hu et al. are unremarkable.

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Figure 1: Characterization of the MeCP2 antibody and MeCP2 coimmunoprecipitates with the Brm-based SWI/SNF complex in NIH3T3 and CEM-CCRF cells but not in HeLaS3 cells.
Figure 2: MeCP2 cofractionates with Brm associated SWI/SNF complex by standard preparative chromatography in human and mouse cells.

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Acknowledgements

We would like to thank H. Zoghbi and T. Cooper for the YB-1 antibody and suggestions.

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Authors and Affiliations

  1. The Alfred Medical Research and Education Precinct (AMREP), Baker Medical Research Institute, Epigenetics in Human Health and Disease Laboratory, Second Floor, Commercial Road, Melbourne, 3004, Victoria, Australia

    KN Harikrishnan, Michael Yarski, Emma K Baker, Maggie Z Chow, Michelle G de Silva, Jun Okabe & Assam El-Osta

  2. Department of Molecular and Cellular Biochemistry, College of Medicine and Public Health, The Ohio State University, Columbus, 43210, Ohio, USA

    Sharmistha Pal, Li Wang & Saïd Sif

  3. Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, 601 S. Goodwin Ave., Urbana, 61802, Illinois, USA

    Peter L Jones

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Supplementary information

Supplementary Fig. 1

Somatic knockdown of MeCP2 in human CEM-CCRF and FRAXA RJK1412 cells illustrates the specificity of MeCP2 siRNA and antibody recognition. (PDF 53 kb)

Supplementary Fig. 2

Isocratic elutions by FPLC on nuclear extracts prepared from human T cell CEM-CCRF G0-arrested cells and peak MeCP2 fractions (combined and immunoprecipitated with antibodies either to MeCP2 or Brm). (PDF 1092 kb)

Supplementary Fig. 3

Colocalization of immunofluorescent MeCP2, Brm and HDAC1 signals in murine and human metaphase chromosomes. (PDF 2407 kb)

Supplementary Table. 1

MeCP2 exists as a multiprotein complex. (PDF 74 kb)

Supplementary Table. 2

Behavior of MeCP2 in neuronal cells and tissues. (PDF 68 kb)

Supplementary Table. 3

Examples of reports in the literature indicating that antibody (N-19, sc-6450) recognizes the Brm epitope in mouse. (PDF 56 kb)

Supplementary Table. 4

Examples of reports in the literature indicate that components of the SWI/SNF complex associate with corepressors or with transcriptional repression. (PDF 88 kb)

Supplementary Note (PDF 189 kb)

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Harikrishnan, K., Pal, S., Yarski, M. et al. Reply to “Testing for association between MeCP2 and the brahma-associated SWI/SNF chromatin-remodeling complex”. Nat Genet 38, 964–967 (2006). https://doi.org/10.1038/ng0906-964

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