Ribosomal protein mRNAs are primary targets of regulation in RNase-L-induced senescence.
Ribosomal protein mRNAs are primary targets of regulation in RNase-L-induced senescence.
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DOI：
10.4161/rna.6.3.8526
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发表时间：
2009-07
期刊：
影响因子：
4.1
通讯作者：
Hassel BA
中科院分区：
文献类型：
--
作者：
Andersen JB;Mazan-Mamczarz K;Zhan M;Gorospe M;Hassel BA
The endoribonuclease RNase-L requires 2′,5′-linked oligoadenylates for activation, and mediates antiviral and antiproliferative activities. We previously determined that RNase-L activation induces senescence; to determine potential mechanisms underlying this activity, we used microarrays to identify RNase-L-regulated mRNAs. RNase-L activation affected affected a finite number of transcripts, and thus does not lead to a global change in mRNA turnover. The largest classes of downregulated transcripts, that represent candidate RNase-L substrates, function in protein biosynthesis, metabolism, and proliferation. Among these, mRNAs encoding ribosomal proteins (RPs) were particularly enriched. The reduced levels of four RP mRNAs corresponded with a decrease in their half lives and a physical association with an RNase-L- ribonucleoprotein (RNP) complex in cells, suggesting that they represent authentic RNase-L substrates. Sequence and structural analysis of the downregulated mRNAs identified a putative RNase-L target motif that was used for the in silico identification of a novel RNase-L-RNP-interacting transcript. The downregulation of RP mRNAs corresponded with a marked reduction in protein translation, consistent with the roles of RP proteins in ribosome function. Our data support a model in which the RNase-L-mediated degradation of RP mRNAs inhibits translation, and may contribute to its antiproliferative, senescence inducing, and tumor suppressor activities.
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