Recent studies invoke phase separation as a mechanism underlying the formation of ‘transcriptional condensates’. However, similarities between transcriptional condensates and the previously introduced ‘transcription factories’ model raise the question of what distinguishes the two models. One crucial aspect to consider is the contribution of intrinsically disordered regions in transcription-relevant factors.
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References
Papantonis, A. & Cook, P. R. Transcription factories: genome organization and gene regulation. Chem. Rev. 113, 8683–8705 (2013).
Rippe, K. Liquid–liquid phase separation in chromatin. Cold Spring Harb. Perspect. Biol. https://doi.org/10.1101/cshperspect.a040683 (2021).
Hnisz, D., Shrinivas, K., Young, R. A., Chakraborty, A. K. & Sharp, P. A. A phase separation model for transcriptional control. Cell 169, 13–23 (2017).
Shrinivas, K. et al. Enhancer features that drive formation of transcriptional condensates. Mol. Cell 75, 549–561 (2019).
Banani, S. F., Lee, H. O., Hyman, A. A. & Rosen, M. K. Biomolecular condensates: organizers of cellular biochemistry. Nat. Rev. Mol. Cell Biol. 18, 285–298 (2017).
Choi, J. M., Holehouse, A. S. & Pappu, R. V. Physical principles underlying the complex biology of intracellular phase transitions. Annu. Rev. Biophys. 49, 107–133 (2020).
Wei, M. T. et al. Nucleated transcriptional condensates amplify gene expression. Nat. Cell Biol. 22, 1187–1196 (2020).
Quintero-Cadena, P., Lenstra, T. L. & Sternberg, P. W. RNA pol II length and disorder enable cooperative scaling of transcriptional bursting. Mol. Cell 79, 207–220 (2020).
Janke, A. M. et al. Lysines in the RNA polymerase II C-terminal domain contribute to TAF15 fibril recruitment. Biochemistry 57, 2549–2563 (2018).
Pontius, B. W. Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association. Trends Biochem. Sci. 18, 181–186 (1993).
Acknowledgements
The work of K.R. on phase separation is funded by the Deutsche Forschungsgemeinschaft (DFG) in Priority Program 2191 ‘Molecular Mechanisms of Functional Phase Separation’ via grant RI1283/16-1. A.P. is also supported by the DFG via the Priority Program 2202 ‘Spatial Genome Architecture in Development and Disease’ (Project 422389065) and the TRR81 Collaborative Research Center (Project 109546710).
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Rippe, K., Papantonis, A. RNA polymerase II transcription compartments: from multivalent chromatin binding to liquid droplet formation?. Nat Rev Mol Cell Biol 22, 645–646 (2021). https://doi.org/10.1038/s41580-021-00401-6
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DOI: https://doi.org/10.1038/s41580-021-00401-6
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