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Corrigendum to “Regulation of RNA Polymerase III Transcription by Maf1 in Mammalian Cells” [J. Mol. Biol. 378(3) (2008) 481–491]
Corrigendum
Corrigendum to “Regulation of RNA Polymerase III Transcription by Maf1 in Mammalian Cells” [J. Mol. Biol. 378(3) (2008) 481–491]
Sarah J. Goodfellow1†, Emma L. Graham1†, Theodoros Kantidakis1,2, Lynne Marshall1,2, Beverly A. Coppins1, Danuta Oficjalska-Pham3,4, Matthieu Gérard5, Olivier Lefebvre3 and Robert J. White1,2 1 - Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK 2 - Beatson Institute for Cancer Research, Switchback Road, Bearsden, Glasgow G61 1BD, UK 3 - Laboratoire de Transcription des Gènes, Service de Biochimie et Génétique Moléculaire, CEA, iBiTecS, F-91191 Gif-sur-Yvette Cedex, France 4 - Department of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland 5 - Laboratoire de Transgenèse, Service de Biologie Moléculaire Systémique, CEA/Saclay, F 91191 Gif-sur-Yvette Cedex, France
Correspondence to Robert J. White: [email protected] DOI of original article: http://dx.doi.org/10.1016/j.jmb.2008.02.060 http://dx.doi.org/10.1016/j.jmb.2012.12.006
The authors have noted an error in Fig. 4 of this article, where the top panels of Fig. 4a and b are the same. We have repeated the experiment and provide a corrected version of the figure, which confirms that Maf1 coimmunoprecipitates with TFIIIC, with or without DNase treatment (Fig. 4a), and in the presence or absence of serum (Fig. 4b). These new experiments use two alternative antisera against Maf1 (1166 and 1167), a positive control immunoprecipitation against TFIIIC, and 4E-BP1 and IgG negative controls. The conditions of the experiment are the same as published and the conclusions are unchanged. We apologize for this mistake. † S.J.G. and E.L.G. contributed equally to this work.
Fig. 4. HsMaf1 associates with TFIIIC. (a) Proteins were immunoprecipitated (IP) from HeLa nuclear extract using the indicated antibodies, in the absence (lanes 2–4 and 8) or presence (lanes 5–7) of 20 U of DNase I. Immunoprecipitates were analysed by Western blotting with a TFIIIC110 antibody from Santa Cruz (sc-81406). Lane 1 shows 10% of input material. (b) Proteins were immunoprecipitated using the indicated antibodies from HeLa cells cultured in the presence of 10% (lanes 3–5) or 0.5% (lanes 6–8) serum. Immunoprecipitates were analysed by Western blotting with a TFIIIC102 antibody from Santa Cruz (sc-101176). Lanes 1 and 2 show 20% of input material. 0022-2836/$ - see front matter © 2012 Elsevier Ltd. All rights reserved.
J. Mol. Biol. (2013) 425, 1099
Corrigendum to “Regulation of RNA Polymerase III Transcription by Maf1 in Mammalian Cells” [J. Mol. Biol. 378(3) (2008) 481–491]
Sarah J. Goodfellow1†, Emma L. Graham1†, Theodoros Kantidakis1,2, Lynne Marshall1,2, Beverly A. Coppins1, Danuta Oficjalska-Pham3,4, Matthieu Gérard5, Olivier Lefebvre3 and Robert J. White1,2 1 - Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK 2 - Beatson Institute for Cancer Research, Switchback Road, Bearsden, Glasgow G61 1BD, UK 3 - Laboratoire de Transcription des Gènes, Service de Biochimie et Génétique Moléculaire, CEA, iBiTecS, F-91191 Gif-sur-Yvette Cedex, France 4 - Department of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland 5 - Laboratoire de Transgenèse, Service de Biologie Moléculaire Systémique, CEA/Saclay, F 91191 Gif-sur-Yvette Cedex, France
Correspondence to Robert J. White: [email protected] DOI of original article: http://dx.doi.org/10.1016/j.jmb.2008.02.060 http://dx.doi.org/10.1016/j.jmb.2012.12.006
The authors have noted an error in Fig. 4 of this article, where the top panels of Fig. 4a and b are the same. We have repeated the experiment and provide a corrected version of the figure, which confirms that Maf1 coimmunoprecipitates with TFIIIC, with or without DNase treatment (Fig. 4a), and in the presence or absence of serum (Fig. 4b). These new experiments use two alternative antisera against Maf1 (1166 and 1167), a positive control immunoprecipitation against TFIIIC, and 4E-BP1 and IgG negative controls. The conditions of the experiment are the same as published and the conclusions are unchanged. We apologize for this mistake. † S.J.G. and E.L.G. contributed equally to this work.
Fig. 4. HsMaf1 associates with TFIIIC. (a) Proteins were immunoprecipitated (IP) from HeLa nuclear extract using the indicated antibodies, in the absence (lanes 2–4 and 8) or presence (lanes 5–7) of 20 U of DNase I. Immunoprecipitates were analysed by Western blotting with a TFIIIC110 antibody from Santa Cruz (sc-81406). Lane 1 shows 10% of input material. (b) Proteins were immunoprecipitated using the indicated antibodies from HeLa cells cultured in the presence of 10% (lanes 3–5) or 0.5% (lanes 6–8) serum. Immunoprecipitates were analysed by Western blotting with a TFIIIC102 antibody from Santa Cruz (sc-101176). Lanes 1 and 2 show 20% of input material. 0022-2836/$ - see front matter © 2012 Elsevier Ltd. All rights reserved.
J. Mol. Biol. (2013) 425, 1099