Sanders, T. et al. FttA is a CPSF73 homologue that terminates transcription in Archaea. Nat. Microbiol. 5, 545â553 (2020).
Yue, L. et al. The conserved ribonuclease aCPSF1 triggers genome-wide transcription termination of Archaea via a 3â²-end cleavage mode. Nucleic Acids Res. 48, 9589â9605 (2020).
Li, J. et al. aCPSF1 cooperates with terminator U-tract to dictate archaeal transcription termination efficacy. eLife 10, e70464 (2021).
Phung, D. et al. Archaeal β-CASP ribonucleases of the aCPSF1 family are orthologs of the eukaryal CPSF-73 factor. Nucleic Acids Res. 41, 1091â1103 (2013).
Nishida, Y. et al. Crystal structure of an archaeal cleavage and polyadenylation specificity factor subunit from Pyrococcus horikoshii. Proteins 78, 2395â2398 (2010).
Mir-Montazeri, B., Ammelburg, M., Forouzan, D., Lupas, A. & Hartmann, M. Crystal structure of a dimeric archaeal cleavage and polyadenylation specificity factor. J. Struct. Biol. 173, 191â195 (2011).
Silva, A. et al. Structure and activity of a novel archaeal beta-CASP protein with N-terminal KH domains. Structure 19, 622â632 (2011).
Fianu, I. et al. Structural basis of Integrator-mediated transcription regulation. Science 374, 883â887 (2021).
Zheng, H. et al. Structural basis of INTAC-regulated transcription. Protein Cell 14, 698â702 (2023).
Fianu, I. et al. Structural basis of Integrator-dependent RNA polymerase II termination. Nature 629, 219â227 (2024).
Lykke-Andersen, S. et al. Integrator is a genome-wide attenuator of non-productive transcription. Mol. Cell 81, 514â529 (2021).
Wagner, E., Tong, L. & Adelman, K. Integrator is a global promoter-proximal termination complex. Mol. Cell 83, 416â427 (2023).
Sun, Y., Hamilton, K. & Tong, L. Recent molecular insights into canonical pre-mRNA 3â²-end processing. Transcription 11, 83â96 (2020).
Eaton, J. & West, S. Termination of transcription by RNA polymerase II. Trends Genet. 36, 664â675 (2020).
Rodriguez-Molina, J., West, S. & Passmore, L. Knowing when to stop: transcription termination on protein-coding genes by eukaryotic RNAPII. Mol. Cell 83, 404â415 (2023).
Boreikaite, V. & Passmore, L. 3â²-End processing of eukaryotic mRNA: machinery, regulation, and impact on gene expression. Ann. Rev. Biochem. 92, 199â225 (2023).
Werner, F. A nexus for gene expression-molecular mechanisms of Spt5 and NusG in the three domains of life. J. Mol. Biol. 417, 13â27 (2012).
Tomar, S. & Artsimovitch, I. NusGâSpt5 proteins-universal tools for transcription modification and communication. Chem. Rev. 113, 8604â8619 (2013).
Song, A. & Chen, F. The pleiotropic roles of SPT5 in transcription. Transcription 13, 53â69 (2022).
Molodtsov, V., Wang, C., Firlar, E., Kaelber, J. & Ebright, R. H. Structural basis of Rho-dependent transcription termination. Nature 614, 367â374 (2023).
Kang, J. et al. Structural basis for transcript elongation control by NusG family universal regulators. Cell 173, 1650â1662 (2018).
Delbeau, M. et al. Structural and functional basis of the universal transcription factor NusG pro-pausing activity in Mycobacterium tuberculosis. Mol. Cell 83, 1474â1488 (2023).
Vishwakarma, R., Qayyum, M., Babitzke, P. & Murakami, K. Allosteric mechanism of transcription inhibition by NusG-dependent pausing of RNA polymerase. Proc. Natl Acad. Sci. USA 120, e2218516120 (2023).
Ehara, H. et al. Structure of the complete elongation complex of RNA polymerase II with basal factors. Science 357, 921â924 (2017).
Wang, C. et al. Structural basis of transcriptionâtranslation coupling. Science 369, 1359â1365 (2020).
Molodtsov, V. et al. Structural basis of RfaH-mediated transcriptionâtranslation coupling. Nature Struct. Mol. Biol. https://doi.org/10.1038/s41594-024-01372-w (2024).
Sun, Y. et al. Structure of an active human histone pre-mRNA 3â²-end processing machinery. Science 367, 700â703 (2020).
Whitelaw, E. & Proudfoot, N. Alpha-thalassaemia caused by a poly(A) site mutation reveals that transcriptional termination is linked to 3â² end processing in the human alpha 2 globin gene. EMBO J. 5, 2915â2922 (1986).
Kim, M. et al. The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II. Nature 432, 517â522 (2004).
West, S., Gromak, N. & Proudfoot, N. Human 5â²â3â² exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites. Nature 432, 522â525 (2004).
Luo, W. & Bentley, D. A ribonucleolytic rat torpedoes RNA polymerase II. Cell 119, 911â914 (2004).
Tollervey, D. Termination by torpedo. Nature 432, 456â457 (2004).
Baejen, C. et al. Genome-wide analysis of RNA polymerase II termination at protein-coding genes. Mol. Cell 66, 38â49.e6 (2017).
Fong, N. et al. Effects of transcription elongation rate and Xrn2 exonuclease activity on RNA polymerase II termination suggest widespread kinetic competition. Mol. Cell 60, 256â267 (2015).
Eaton, J. et al. Xrn2 accelerates termination by RNA polymerase II, which is underpinned by CPSF73 activity. Genes Dev. 32, 127â139 (2018).
Cortazar, M. et al. Xrn2 substrate mapping identifies torpedo loading sites and extensive premature termination of RNA pol II transcription. Genes Dev. 36, 1062â1078 (2022).
Zeng, Y., Zhang, H. W., Wu, X. X. & Zhang, Y. Structural basis of exoribonuclease-mediated mRNA transcription termination. Nature 628, 887â893 (2024).
Yanagisawa, T. et al. Structural basis of eukaryotic transcription termination by the Rat1 exonuclease complex. Preprint at bioRxiv https://doi.org/10.1101/2024.03.28.587100 (2024).
Larson, M., Greenleaf, W., Landick, R. & Block, S. Applied force reveals mechanistic and energetic details of transcription termination. Cell 132, 971â982 (2008).
Santangelo, T. & Roberts, J. Forward translocation is the natural pathway of RNA release at an intrinsic terminator. Mol. Cell 14, 117â126 (2004).
Park, J. & Roberts, J. Role of DNA bubble rewinding in enzymatic transcription termination. Proc. Natl Acad. Sci. USA 103, 4870â4875 (2006).
Ray-Soni, A., Bellecourt, M. & Landick, R. Mechanisms of bacterial transcription termination. Annu. Rev. Biochem. 85, 319â347 (2016).
Roberts, J. Mechanisms of bacterial transcription termination. J. Mol. Biol. 431, 4030â4039 (2019).
Epshtein, V., Cardinale, C., Ruckenstein, A., Borukhov, S. & Nudler, E. An allosteric path to transcription termination. Mol. Cell 28, 991â1001 (2007).
Epshtein, V., Dutta, D., Wade, J. & Nudler, E. An allosteric mechanism of Rho-dependent transcription termination. Nature 463, 245â249 (2010).
Webster, M. et al. Structural basis of transcriptionâtranslation coupling and collision in bacteria. Science 369, 1355â1359 (2020).
Blaha, G. & Wade, J. Transcriptionâtranslation coupling in bacteria. Annu. Rev. Genet. 56, 9.1â9.19 (2022).
French, S., Santangelo, T., Beyer, A. & Reeve, J. Transcription and translation are coupled in Archaea. Mol. Biol. Evol. 24, 893â895 (2007).
Weixlbaumer, A., Grunberger, F., Werner, F. & Grohmann, D. Coupling of transcription and translation in archaea: cues from the bacterial world. Front. Microbiol. 12, 661827 (2021).
Grana, D., Gardella, T. & Susskind, M. The effects of mutations in the ant promoter of phage P22 depend on context. Genet. 120, 319â327 (1988).
Sambrook, J., Fritsch, E. & Maniatis, T. Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Laboratory, 1989).
Punjani, A., Rubinstein, J., Fleet, D. & Brubaker, M. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290â296 (2017).
Pettersen, E. et al. UCSF chimera: a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605â1612 (2004).
Jun, S.-H. et al. Direct binding of TFEα opens DNA binding cleft of RNA polymerase. Nat. Commun. 11, 6123 (2020).
Klein, B. J. et al. RNA polymerase and transcription elongation factor Spt4/5 complex structure. Proc. Natl Acad. Sci. USA 108, 46â550 (2011).
Emsley, P., Lohkamp, B., Scott, W. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486â501 (2010).
Afonine, T., Headd, J., Terwilliger, T. & Adams, P. Computational Crystallography Newsletter 4, 43â44; https://phenix-online.org/phenixwebsite_static/mainsite/files/newsletter/CCN_2013_07.pdf (2013).
Suloway, C. et al. Automated molecular microscopy: the new Leginon system. J. Struct. Biol. 151, 41â60 (2005).