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The mutation nrpb1‐A325V in the largest subunit of RNA polymerase II suppresses compromised growth of Arabidopsis plants deficient in a function of the general transcription factor IIF
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Elena Babiychuk Khai Trinh Hoang Klaas Vandepoele Eveline Van De Slijke Danny Geelen Geert De Jaeger Junichi Obokata Sergei Kushnir 《The Plant journal : for cell and molecular biology》2017,89(4):730-745
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Abscisic acid affects transcription of chloroplast genes via protein phosphatase 2C‐dependent activation of nuclear genes: repression by guanosine‐3′‐5′‐bisdiphosphate and activation by sigma factor 5
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Maria V. Yamburenko Yan O. Zubo Thomas Börner 《The Plant journal : for cell and molecular biology》2015,82(6):1030-1041
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RNA polymerase II acts as an RNA‐dependent RNA polymerase to extend and destabilize a non‐coding RNA
Steven L Ponicsan Linda F Drullinger Jennifer F Kugel James A Goodrich 《The EMBO journal》2013,32(6):781-790
RNA polymerase II (Pol II) is a well‐characterized DNA‐dependent RNA polymerase, which has also been reported to have RNA‐dependent RNA polymerase (RdRP) activity. Natural cellular RNA substrates of mammalian Pol II, however, have not been identified and the cellular function of the Pol II RdRP activity is unknown. We found that Pol II can use a non‐coding RNA, B2 RNA, as both a substrate and a template for its RdRP activity. Pol II extends B2 RNA by 18 nt on its 3′‐end in an internally templated reaction. The RNA product resulting from extension of B2 RNA by the Pol II RdRP can be removed from Pol II by a factor present in nuclear extracts. Treatment of cells with α‐amanitin or actinomycin D revealed that extension of B2 RNA by Pol II destabilizes the RNA. Our studies provide compelling evidence that mammalian Pol II acts as an RdRP to control the stability of a cellular RNA by extending its 3′‐end. 相似文献
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