期刊
MOLECULAR CELL
卷 81, 期 15, 页码 3110-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2021.06.016
关键词
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资金
- Joachim Hertz Stiftung
- German Research Foundation (DFG) [WO 2108/1-1, GRK 2243, ER 927/2-1]
- German Cancer Aid (MSNZ)
- European Research Council
SPT6 is crucial for RNAPII processivity and productive transcription of protein-coding genes, as well as for RNAPII termination. Long-term depletion of SPT6 induces cryptic intragenic transcription.
SPT6 is a histone chaperone that tightly binds RNA polymerase II (RNAPII) during transcription elongation. However, its primary role in transcription is uncertain. We used targeted protein degradation to rapidly deplete SPT6 in human cells and analyzed defects in RNAPII behavior by a multi-omics approach and mathematical modeling. Our data indicate that SPT6 is a crucial factor for RNAPII processivity and is therefore required for the productive transcription of protein-coding genes. Unexpectedly, SPT6 also has a vital role in RNAPII termination, as acute depletion induced readthrough transcription for thousands of genes. Long-term depletion of SPT6 induced cryptic intragenic transcription, as observed earlier in yeast. However, this phenotype was not observed upon acute SPT6 depletion and therefore can be attributed to accumulated epigenetic perturbations in the prolonged absence of SPT6. In conclusion, targeted degradation of SPT6 allowed the temporal discrimination of its function as an epigenetic safeguard and RNAPII elongation factor.
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