Genome-wide analysis of RNA polymerase II termination at protein-coding genes.

Bäjen, C.; Andreani, J.; Torkler, P.; Battaglia, S.; Schwalb, B.; Lidschreiber, M.; Maier, K. C.; Boltendahl, A.; Rus, P.; Esslinger, S.; Söding, J.; Cramer, P.

doi:10.1016/j.molcel.2017.02.009

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Genome-wide analysis of RNA polymerase II termination at protein-coding genes.

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Bäjen, C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Andreani, J.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Torkler, P.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Battaglia, S.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Schwalb, B.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Lidschreiber, M.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Maier, K. C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons203889

Boltendahl, A.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Rus, P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Söding, J.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Cramer, P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Zitation

Bäjen, C., Andreani, J., Torkler, P., Battaglia, S., Schwalb, B., Lidschreiber, M., et al. (2017). Genome-wide analysis of RNA polymerase II termination at protein-coding genes. Molecular Cell, 66(1), 38-49. doi:10.1016/j.molcel.2017.02.009.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002C-DD60-9

Zusammenfassung

At the end of protein-coding genes, RNA polymerase (Pol) II undergoes a concerted transition that involves 3′-processing of the pre-mRNA and transcription termination. Here, we present a genome-wide analysis of the 3′-transition in budding yeast. We find that the 3′-transition globally requires the Pol II elongation factor Spt5 and factors involved in the recognition of the polyadenylation (pA) site and in endonucleolytic RNA cleavage. Pol II release from DNA occurs in a narrow termination window downstream of the pA site and requires the “torpedo” exonuclease Rat1 (XRN2 in human). The Rat1-interacting factor Rai1 contributes to RNA degradation downstream of the pA site. Defects in the 3′-transition can result in increased transcription at downstream genes.