Purification and properties of HuD, a neuronal RNA-binding protein Journal Article


Authors: Chung, S.; Jiang, L.; Cheng, S.; Furneaux, H.
Article Title: Purification and properties of HuD, a neuronal RNA-binding protein
Abstract: HuD is a human neuronal specific RNA-binding protein. In this study we have purified HuD and examined its RNA binding properties in detail. HuD binds to mRNAs that contain an AU-rich element with high affinity. In the case of the c-fos AU-rich element, HuD binds to a 27-nucleotide core element comprising AUUUA, AUUUUA, and AUUUUUA motifs. Mutation in any two of these motifs abrogates binding. HuD contains two tandem RNA recognition motifs (RRM), a basic domain, and a third RRM. Deletion analysis has shown that only the first and second RRMs are essential for RNA binding. Thus, these specific RNA binding properties support the idea that the HuD regulates gene expression at the posttranscriptional level.
Keywords: gene mutation; nonhuman; binding affinity; polymerase chain reaction; protein analysis; complex formation; neurons; cell specificity; rna binding protein; cloning, molecular; rna-binding proteins; molecular sequence data; recombinant fusion proteins; protein purification; rna, messenger; escherichia coli; substrate specificity; base sequence; binding protein; binding site; binding sites; nerve cell; rna binding; complementary dna; dna, complementary; globins; proto-oncogene proteins c-fos; humans; priority journal; article; oncogene c fos; genes, fos; ribonuclease t1
Journal Title: Journal of Biological Chemistry
Volume: 271
Issue: 19
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 1996-05-10
Start Page: 11518
End Page: 11524
Language: English
DOI: 10.1074/jbc.271.19.11518
PUBMED: 8626712
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 22 November 2017 -- Source: Scopus
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