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44. Structural insights into transcription complexes

Author

Berger, I., Blanco, A.G., Boelens, R., Cavarelli, J., Coll, M., Folkers, G.E., Nie, Y., Pogenberg, V., Schultz, P., Wilmanns, M., Moras, D., Poterszman, A., NMR Spectroscopy, Sub NMR Spectroscopy, NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
Magnetic Resonance Spectroscopy, Transcription, Genetic, Protein Conformation, Receptors, Cytoplasmic and Nuclear, Transcription coregulator, Biology, Crystallography, X-Ray, Epigenesis, Genetic, Allosteric Regulation, Structural Biology, Transcription (biology), Transcription factors, Animals, Humans, Regulation of gene expression, Promoter Regions, Genetic, Transcription factor, General transcription factor, Multi-subunit complexes, Eukaryotic transcription, Cryoelectron Microscopy, Structural proteomics, Cell biology, Structural biology, Multiprotein Complexes, Transcription factor II H, Transcription factor II D, Transcription Factors
Abstract

Control of transcription allows the regulation of cell activity in response to external stimuli and research in the field has greatly benefited from efforts in structural biology. In this review, based on specific examples from the European SPINE2-COMPLEXES initiative, we illustrate the impact of structural proteomics on our understanding of the molecular basis of gene expression. While most atomic structures were obtained by X-ray crystallography, the impact of solution NMR and cryo-electron microscopy is far from being negligible. Here, we summarize some highlights and illustrate the importance of specific technologies on the structural biology of protein-protein or protein/DNA transcription complexes: structure/function analysis of components the eukaryotic basal and activated transcription machinery with focus on the TFIID and TFIIH multi-subunit complexes as well as transcription regulators such as members of the nuclear hormone receptor families. We also discuss molecular aspects of promoter recognition and epigenetic control of gene expression. © 2011 Elsevier Inc., This work forms part of SPINE2-complexes Contract No. LSHG-CT-2006-031220, funded by the European Commission under the Integrated Programme ‘Quality of Life and Management of Living Resources’. This work was also supported by grants from the EC FP7 IS project P-CUBE (to I.B.), from the Spanish ‘Ministerio de Ciencia e Innovación’ (Grants BFU2008-02372/BMC and CSD2006-00023) and the ‘Generalitat de Catalunya’ (Grant 2009SGR-1309) (to A.B. and M.C.), from the Netherlands Organisation for Scientific Research, Division of Chemical Sciences, NWO-CW (to R.B.) and from the Agence Nationale de la Recherche, the Association de la Recherche sur le Cancer and the Institut National du Cancer (to J.C., P.S, D.M. and A.P.).

Published
2011

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