Authors: | Joseph, B.; Orlian, M.; Furneaux, H. |
Article Title: | p21(waf1) mRNA contains a conserved element in its 3'-untranslated region that is bound by the Elav-like mRNA-stabilizing proteins |
Abstract: | The Elav-like proteins are specific mRNA-binding proteins that regulate mRNA stability. The neuronal members of this family (HuD, HuC, and Hel-N1) are required for neuronal differentiation. In this report, using purified HuD protein we have localized a high affinity HuD binding site to a 42-nucleotide region within a U-rich tract in the 3'-untranslated region p21(waf1) mRNA. The binding of HuD to this site is readily displaced by an RNA oligonucleotide encoding the HuD binding site of c-los. The sequence of this binding site is well conserved in human, mouse, and rat p21(waf1) mRNA. p21(waf1) is an inhibitor of cyclin-dependent kinases and proliferating cell nuclear antigen and induces cell cycle arrest at G1/S, a requisite early step in cell differentiation. The identification of an Elav-like protein binding site in the 3'-untranslated region of p21(waf1) provides a novel link between the induction of differentiation, mRNA stability, and the termination of the cell cycle. |
Keywords: | sequence analysis; animals; mice; cell cycle; nerve tissue proteins; protein stability; cell differentiation; rna-binding proteins; conserved sequence; molecular sequence data; messenger rna; enzyme inhibitors; rna, messenger; ribonucleoproteins; base sequence; binding site; binding sites; rats; cyclin-dependent kinase inhibitor p21; protein structure; structure analysis; cyclin-dependent kinases; cyclins; protein p21; hu paraneoplastic encephalomyelitis antigens; ribonucleases; rna binding; rna sequence; oligonucleotides; binding, competitive; mitosis inhibition; humans; priority journal; article; genes, fos |
Journal Title: | Journal of Biological Chemistry |
Volume: | 273 |
Issue: | 32 |
ISSN: | 0021-9258 |
Publisher: | American Society for Biochemistry and Molecular Biology |
Date Published: | 1998-08-07 |
Start Page: | 20511 |
End Page: | 20516 |
Language: | English |
DOI: | 10.1074/jbc.273.32.20511 |
PUBMED: | 9685407 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Article -- Export Date: 12 December 2016 -- Source: Scopus |