Novel recognition motifs and biological functions of the RNA-binding protein HuD revealed by genome-wide identification of its targets

We have investigated the RNA binding specificity of Hel-N1, a human neuron-specific RNA-binding protein, which contains three RNA recognition motifs. Hel-N1 is a human homolog of Drosophila melanogaster elav, which plays a vital role in the development of neurons. A random RNA selection procedure revealed that Hel-N1 prefers to bind RNAs containing short stretches of uridylates similar to those found in the 3' untranslated regions (3' UTRs) of oncoprotein and cytokine mRNAs such as c-myc, c-fos, and granulocyte macrophage colony-stimulating factor. Direct binding studies demonstrated that Hel-N1 bound and formed multimers with c-myc 3' UTR mRNA and required, as a minimum, a specific 29-nucleotide stretch containing AUUUG, AUUUA, and GUUUUU. Deletion analysis demonstrated that a fragment of Hel-N1 containing 87 amino acids, encompassing the third RNA recognition motif, forms an RNA binding domain for the c-myc 3' UTR. In addition, Hel-N1 was shown to be reactive with autoantibodies from patients with paraneoplastic encephalomyelitis both before and after binding to c-myc mRNA.

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Genome-wide survey of putative RNA-binding proteins encoded in the human proteome

Molecular BioSystems ◽

10.1039/c5mb00638d ◽

2016 ◽

Vol 12 (2) ◽

pp. 532-540 ◽

Cited By ~ 16

Author(s):

Pritha Ghosh ◽

R. Sowdhamini

Keyword(s):

Binding Proteins ◽

Rna Binding ◽

Rna Binding Proteins ◽

Binding Protein ◽

Rna Binding Protein ◽

Human Proteome ◽

Genome Wide ◽

Genome Wide Survey

We have classified the existing RNA-binding protein (RBP) structures into different structural families. Here, we report ∼2600 proteins with RBP signatures in humans.

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Genome-Wide Identification, Biochemical Characterization, and Expression Analyses of the YTH Domain-Containing RNA-Binding Protein Family in Arabidopsis and Rice

Plant Molecular Biology Reporter ◽

10.1007/s11105-014-0724-2 ◽

2014 ◽

Vol 32 (6) ◽

pp. 1169-1186 ◽

Cited By ~ 25

Author(s):

Dayong Li ◽

Huijuan Zhang ◽

Yongbo Hong ◽

Lei Huang ◽

Xiaohui Li ◽

...

Keyword(s):

Rna Binding ◽

Biochemical Characterization ◽

Binding Protein ◽

Rna Binding Protein ◽

Protein Family ◽

Genome Wide ◽

Yth Domain

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Genome-wide identification and expression analysis of YTH domain-containing RNA-binding protein family in cucumber (Cucumis sativus)

Genes & Genomics ◽

10.1007/s13258-018-0659-3 ◽

2018 ◽

Vol 40 (6) ◽

pp. 579-589 ◽

Cited By ~ 4

Author(s):

Yong Zhou ◽

Lifang Hu ◽

Lunwei Jiang ◽

Shiqiang Liu

Keyword(s):

Cucumis Sativus ◽

Expression Analysis ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Protein Family ◽

Genome Wide ◽

Yth Domain

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Hel-N1: an autoimmune RNA-binding protein with specificity for 3' uridylate-rich untranslated regions of growth factor mRNAs

Molecular and Cellular Biology ◽

10.1128/mcb.13.6.3494-3504.1993 ◽

1993 ◽

Vol 13 (6) ◽

pp. 3494-3504

Author(s):

T D Levine ◽

F Gao ◽

P H King ◽

L G Andrews ◽

J D Keene

Keyword(s):

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Selection Procedure ◽

Vital Role ◽

Untranslated Regions ◽

Rna Recognition Motif ◽

Rna Recognition ◽

Binding Studies ◽

Recognition Motifs

We have investigated the RNA binding specificity of Hel-N1, a human neuron-specific RNA-binding protein, which contains three RNA recognition motifs. Hel-N1 is a human homolog of Drosophila melanogaster elav, which plays a vital role in the development of neurons. A random RNA selection procedure revealed that Hel-N1 prefers to bind RNAs containing short stretches of uridylates similar to those found in the 3' untranslated regions (3' UTRs) of oncoprotein and cytokine mRNAs such as c-myc, c-fos, and granulocyte macrophage colony-stimulating factor. Direct binding studies demonstrated that Hel-N1 bound and formed multimers with c-myc 3' UTR mRNA and required, as a minimum, a specific 29-nucleotide stretch containing AUUUG, AUUUA, and GUUUUU. Deletion analysis demonstrated that a fragment of Hel-N1 containing 87 amino acids, encompassing the third RNA recognition motif, forms an RNA binding domain for the c-myc 3' UTR. In addition, Hel-N1 was shown to be reactive with autoantibodies from patients with paraneoplastic encephalomyelitis both before and after binding to c-myc mRNA.

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