An RNA-protein complex links enhanced nuclear 3′ processing with cytoplasmic mRNA stabilization
An RNA-protein complex links enhanced nuclear 3′ processing with cytoplasmic mRNA stabilization
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DOI:
10.1038/emboj.2011.171
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发表时间:
2011-07-06
期刊:
影响因子:
11.4
通讯作者:
Liebhaber, Stephen A.
中科院分区:
文献类型:
--
作者:
Ji, Xinjun;Kong, Jian;Liebhaber, Stephen A.
Post-transcriptional controls are critical to gene regulation. These controls are frequently based on sequence-specific binding of trans-acting proteins to cis-acting motifs on target RNAs. Prior studies have revealed that the KH-domain protein, alpha CP, binds to a 3' UTR C-rich motif of h alpha-globin mRNA and contributes to its cytoplasmic stability. Here, we report that this 3' UTR alpha CP complex regulates the production of mature alpha-globin mRNA by enhancing 3' processing of the h alpha-globin transcript. We go on to demonstrate that this nuclear activity reflects enhancement of both the cleavage and the polyadenylation reactions and that alpha CP interacts in vivo with core components of the 3' processing complex. Consistent with its nuclear processing activity, our studies reveal that alpha CP assembles co-transcriptionally at the h alpha-globin chromatin locus and that this loading is selectively enriched at the 3' terminus of the gene. The demonstrated linkage of nuclear processing with cytoplasmic stabilization via a common RNA-protein complex establishes a basis for integration of sequential controls critical to robust and sustained expression of a target mRNA. The EMBO Journal (2011) 30, 2622-2633. doi:10.1038/emboj.2011.171; Published online 27 May 2011