| pubmed-article:8890177 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8890177 | lifeskim:mentions | umls-concept:C0066030 | lld:lifeskim |
| pubmed-article:8890177 | lifeskim:mentions | umls-concept:C0015219 | lld:lifeskim |
| pubmed-article:8890177 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:8890177 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:8890177 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:8890177 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:8890177 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:8890177 | lifeskim:mentions | umls-concept:C1504308 | lld:lifeskim |
| pubmed-article:8890177 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:8890177 | pubmed:dateCreated | 1996-12-10 | lld:pubmed |
| pubmed-article:8890177 | pubmed:abstractText | RNA-protein (RNP) complexes play significant roles in the fate and expression of mRNAs. The prolonged half-life of human alpha-globin mRNA, a major determinant of normal erythroid differentiation, is dependent on the assembly of a sequence-specific 3'-untranslated region (3'UTR) RNP (alpha-complex). We demonstrate that the stability of murine alpha-globin mRNA is controlled by a parallel mechanism. Unexpectedly, however, the respective 3'UTR RNP complexes that stabilize the h(alpha)- and m(alpha)-globin mRNAs differ in structure. While the cis determinants in both species are encoded in polypyrimidine tracks, the human determinant is C-rich (CCUCC motif) while the mouse alpha-3'UTR consists of an equal distribution of Cs and Us (CCUUCU motif). The protein components of the corresponding human and murine alpha-complexes differ in a complementary manner: the previously described 39 kDa poly(C) binding protein (PCBP) present in the human alpha-complex is replaced in the mouse alpha-complex by a 48 kDa cytoplasmic poly(CU) binding protein (CUBP). These results reveal that drift in the primary sequences of the alpha-globin mRNA 3'UTR polypyrimidine tracks in a comparison between mouse and human is paralleled by an alteration in the composition of the corresponding trans-acting components. Surprisingly, these structurally distinct complexes appear to perform the identical function of stabilizing the corresponding alpha-globin mRNAs. | lld:pubmed |
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| pubmed-article:8890177 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8890177 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8890177 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8890177 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8890177 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8890177 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8890177 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8890177 | pubmed:author | pubmed-author:LiebhaberS... | lld:pubmed |
| pubmed-article:8890177 | pubmed:author | pubmed-author:WangXX | lld:pubmed |
| pubmed-article:8890177 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8890177 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:8890177 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:8890177 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8890177 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8890177 | pubmed:pagination | 5040-51 | lld:pubmed |
| pubmed-article:8890177 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
