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首页> 外文期刊>Molecular and Cellular Biology >Detection and characterization of a 3' untranslated region ribonucleoprotein complex associated with human alpha-globin mRNA stability.
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Detection and characterization of a 3' untranslated region ribonucleoprotein complex associated with human alpha-globin mRNA stability.

机译：3'非翻译区核糖核蛋白复合体与人类α-珠蛋白mRNA稳定性相关的检测和表征。

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The highly stable nature of globin mRNA is of central importance to erythroid cell differentiation. We have previously identified cytidine-rich (C-rich) segments in the human alpha-globin mRNA 3' untranslated region (alpha-3'UTR) which are critical in the maintenance of mRNA stability in transfected erythroid cells. In the present studies, we have detected trans-acting factors which interact with these cis elements to mediate this stabilizing function. A sequence-specific ribonucleoprotein (RNP) complex is assembled after incubation of the alpha-3'UTR with a variety of cytosolic extracts. This so-called alpha-complex is sequence specific and is not formed on the 3'UTR of either beta-globin or growth hormone mRNAs. Furthermore, base substitutions within the C-rich stretches which destabilize alpha-globin mRNA in vivo result in a parallel disruption of the alpha-complex in vitro. Competition studies with a series of homoribopolymers reveals a striking sensitivity of alpha-complex formation to poly(C), suggesting the presence of a poly(C)-binding activity within the alpha-complex. Three predominant proteins are isolated by alpha-3'UTR affinity chromatography. One of these binds directly to poly(C). This cytosolic poly(C)-binding protein is distinct from previously described nuclear poly(C)-binding heterogeneous nuclear RNPs and is necessary but not sufficient for alpha-complex formation. These data suggest that a messenger RNP complex formed by interaction of defined segments within the alpha-3'UTR with a limited number of cytosolic proteins, including a potentially novel poly(C)-binding protein, is of functional importance in establishing high-level stability of alpha-globin mRNA.
机译：珠蛋白mRNA的高度稳定的性质对红系细胞分化至关重要。我们以前已经确定了人类α-珠蛋白mRNA 3'非翻译区（alpha-3'UTR）中富含胞苷的片段（富含C的片段），这对于维持转染的类红细胞中的mRNA稳定性至关重要。在本研究中，我们已经检测到与这些顺式元件相互作用的反式作用因子，以介导这种稳定功能。在将alpha-3'UTR与多种胞质提取物孵育后，将组装具有序列特异性的核糖核蛋白（RNP）复合物。这种所谓的α-复合物是序列特异性的，不会在β-珠蛋白或生长激素mRNA的3'UTR上形成。此外，富含C的链段内的碱基取代在体内使α-珠蛋白mRNA不稳定，从而导致体外的α-复合物平行破坏。一系列同型核聚合物的竞争研究表明，α-复合物形成对poly（C）的惊人敏感性，表明在α-复合物中存在poly（C）结合活性。通过alpha-3'UTR亲和层析分离了三种主要的蛋白质。其中之一直接与poly（C）结合。该胞质多聚（C）结合蛋白不同于先前描述的核聚（C）结合异质核RNP，并且对于形成α-复合物而言是必需的，但不足。这些数据表明，由alpha-3'UTR中的限定片段与有限数量的胞质蛋白（包括潜在的新型聚（C）结合蛋白）相互作用形成的信使RNP复合物在建立高水平的功能方面具有重要的功能。 α-珠蛋白mRNA的稳定性。

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