Selected article for: "mRNA decay and stem loop"
Author: Su, Junhui; Chang, Cui; Xiang, Qi; Zhou, Zhi-Wei; Luo, Rong; Yang, Lun; He, Zhi-Xu; Yang, Hongtu; Li, Jianan; Bei, Yu; Xu, Jinmei; Zhang, Minjing; Zhang, Qihao; Su, Zhijian; Huang, Yadong; Pang, Jiyan; Zhou, Shu-Feng
Title: Xyloketal B, a marine compound, acts on a network of molecular proteins and regulates the activity and expression of rat cytochrome P450 3a: a bioinformatic and animal study
  • Document date: 2014_12_12
    • ID: y14atmnh_90
    Snippet: RNA exonuclease that binds to the 3′-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication; 2′-hydroxyl and 3′-hydroxyl groups at the last nucleotide of the histone 3′-end is required for efficient degradation of RNA substrates. Also able to degrade the 3′-overhangs of small interfering RNAs in vitro, suggesting a possible role as a regulator of RNA interference. Requi.....
    Document: RNA exonuclease that binds to the 3′-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication; 2′-hydroxyl and 3′-hydroxyl groups at the last nucleotide of the histone 3′-end is required for efficient degradation of RNA substrates. Also able to degrade the 3′-overhangs of small interfering RNAs in vitro, suggesting a possible role as a regulator of RNA interference. Required for binding the 5′-ACCCA-3′ sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8 SrRNA 3′-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replicationdependent histone pre-mRNAs.

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