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A novel RNA‐binding domain in the nuclear export factor (NXF) family
Author(s) -
Kerkow Donald E,
Baca Jacqueline E,
Williamson James R
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.2_supplement.211
Subject(s) - nuclear export signal , rna binding protein , rna , messenger rna , untranslated region , biology , microbiology and biotechnology , three prime untranslated region , genetics , chemistry , gene
The first step governing mRNA export and metabolism is the sorting of processed transcripts into specific nuclear export pathways. The nuclear export factor (NXF) family orchestrates general mRNA nuclear export as well as tissue and substrate specific RNA regulation. However, it is not fully understood how NXF proteins interact with mRNA or if direct mRNA binding by NXF proteins is required for mRNA nuclear export. Here, we show that the highly conserved NTF2‐like domain of the NXF family exhibits novel RNA binding activity. Quantitative experiments with two NXF family members, C. elegans NXF‐2 (CeNXF‐2) and human NXF1 (HsNXF1), reveal that the NXF NTF2‐like domain binds RNA with high affinity and has specificity for tracts of uridine residues. We find that CeNXF‐2's NTF2‐like domain is both necessary and sufficient for high affinity binding to the 3′ UTR of the transformer‐2 ( tra‐2 ) mRNA, which is critical in C. elegans sexual development. Homology modeling of CeNXF‐2's NTF2‐like domain, based on the structure of HsNXF1, identifies two potential RNA binding surfaces. Overall, our data suggest that the NTF2‐like fold, ubiquitous in the NXF family, has a conserved yet previously unseen RNA binding function, which likely plays an important role in mRNA recognition and export.