Authors: | Haeussler, J.; Haeusler, J.; Striebel, A. M.; Assum, G.; Vogel, W.; Furneaux, H.; Krone, W. |
Article Title: | Tumor antigen HuR binds specifically to one of five protein-binding segments in the 3'-untranslated region of the neurofibromin messenger RNA |
Abstract: | 3'-untranslated regions of various mRNAs have been shown to contain sequence motifs which control mRNA stability, translatability, and efficiency of translation as well as intracellular localization. We aimed to identify protein binding regions of the long and highly conserved 3'UTR of the mRNA coding for neurofibromin, a well-known tumor suppressor protein, whose genetic deficiency causes the autosomal dominant disease neurofibromatosis type 1 (NF1). We discovered five RNA fragments that were able to undergo specific binding to proteins from cell lysates (NF1-PBRs, NF1-protein-binding regions). Additionally we identified the Elav-like protein HuR binding to NF1-PBR1. HuR interacts with AU-rich elements in the 3'UTR of many protooncogenes, cytokines, and transcription factors, thereby regulating the expression of these mRNAs on the posttranscriptional level. Transfection assays with a CAT reporter construct revealed reduced expression of the reporter, suggesting that HuR may be involved in the fine-tuning of the expression of the NF1 gene. (C) 2000 Academic Press. |
Keywords: | controlled study; human cell; gene deletion; proteins; neurofibromatosis; proto oncogene; nerve tissue proteins; protein binding; transcription factor; transcription, genetic; hela cells; transfection; tumor antigen; rna-binding proteins; cytokine; genetic transfection; messenger rna; rna, messenger; fibroblasts; rna translation; neurofibromin; neurofibromin 1; binding sites; antigen binding; antigens, surface; cell lysate; 3' untranslated regions; rna sequence; protein rna binding; open reading frames; messenger rna synthesis; humans; human; priority journal; article; chloramphenicol o-acetyltransferase |
Journal Title: | Biochemical and Biophysical Research Communications |
Volume: | 267 |
Issue: | 3 |
ISSN: | 0006-291X |
Publisher: | Elsevier Science, Inc. |
Date Published: | 2000-01-27 |
Start Page: | 726 |
End Page: | 732 |
Language: | English |
DOI: | 10.1006/bbrc.1999.2019 |
PUBMED: | 10673359 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Export Date: 18 November 2015 -- Source: Scopus |