The Elav-like proteins bind to a conserved regulatory element in the 3'- untranslated region of GAP-43 mRNA Journal Article

  


Authors: Chung, S.; Eckrich, M.; Perrone-Bizzozero, N.; Kohn, D. T.; Furneaux, H.
Article Title: The Elav-like proteins bind to a conserved regulatory element in the 3'- untranslated region of GAP-43 mRNA
Abstract: Previous studies have identified three brain proteins (40, 65 and 95 kDa, respectively) that specifically bind to the 3'-untranslated region of GAP-43 mRN. In this study, using a specific monoclonal antibody, we now show that the 40-kDa proteins are members of the Elav-like protein family. This family of specific RNA-binding proteins comprise three neural specific members called HuD, HuC, and Hel-N1. We have shown that purified recombinant HuD can bind with high affinity to GAP-43 mRNA. In addition, we have mapped the binding site to a highly conserved 26-nucleotide sequence within the regulatory element. The binding of HuD to this site is readily displaced by RNA oligonucleotides encoding other HuD binding sites. We also show that only the first and second RNA binding domains of HuD are required for selective binding to GAP-43 mRNA.
Keywords: nonhuman; animals; cell function; nerve tissue proteins; monoclonal antibody; gene expression regulation; rna-binding proteins; gene mapping; transcription regulation; molecular sequence data; messenger rna; rna, messenger; membrane glycoproteins; nucleotide sequence; recombinant proteins; base sequence; binding protein; binding site; antibody specificity; rats; protein family; nerve cell differentiation; genetic conservation; neuroblast; gap-43 protein; hu paraneoplastic encephalomyelitis antigens; regulatory sequences, nucleic acid; protein synthesis regulation; binding, competitive; priority journal; article
Journal Title: Journal of Biological Chemistry
Volume: 272
Issue: 10
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 1997-03-07
Start Page: 6593
End Page: 6598
Language: English
DOI: 10.1074/jbc.272.10.6593
PUBMED: 9045688
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030937588&doi=10.1074%2fjbc.272.10.6593&partnerID=40&md5=5cd49f8b05629f3736f7b7be97826a21
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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MSK Authors
  1. Henry M Furneaux
    57 Furneaux
  2. Michael J Eckrich
    1 Eckrich
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