期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 23, 期 4, 页码 1125-1134出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.23.4.1125-1134.2003
关键词
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资金
- NCI NIH HHS [P01 CA072765, CA72765] Funding Source: Medline
- NHLBI NIH HHS [R01 HL065449, HL 65449, R37 HL065449] Funding Source: Medline
Previous studies suggest that high-level stability of a subset of mammalian mRNAs is linked to a C-rich motif in the 3' untranslated region (3'UTR). High-level expression of human alpha-globin mRNA (hot-globin mRNA) in erythroid cells has been specifically attributed to formation of an RNA-protein complex comprised of a 3'UTR C-rich motif and an associated 39-kDa poly(C) binding protein, alphaCP. Documentation of this RNA-protein alpha-complex has been limited to in vitro binding studies, and its impact has been monitored by alterations in steady-state mRNA. Here we demonstrate that alphaCP is stably bound to hot-globin mRNA in vivo, that alpha-complex assembly on the hot-globin mRNA is restricted to the 3'UTR C-rich motif, and that alpha-complex assembly extends the physical half-life of hot-globin mRNA selectively in erythroid cells. Significantly, these studies also reveal that an artificially tethered alphaCP has the same mRNA-stabilizing activity as the native alpha-complex. These data demonstrate a unique contribution of the alpha-complex to hot-globin mRNA stability and support a model in which the sole function of the C-rich motif is to selectively tether alphaCP to a subset of mRNAs. Once bound, alphaCP appears to be fully sufficient to trigger downstream events in the stabilization pathway.
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