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Quality control of mRNA export: An evolutionarily conserved zinc finger protein mediates preferential export of properly processed mRNA to the cytoplasm
Author(s) -
Corbett Anita H,
Kelly Seth M,
Fasken Milo B,
Leung Sara W,
Stewart Murray
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.22.1_supplement.992.1
Subject(s) - zinc finger , nuclear export signal , messenger rna , rna binding protein , lim domain , microbiology and biotechnology , biology , polyadenylation , rna , mature messenger rna , cytoplasm , cell nucleus , gene , genetics , rna splicing , transcription factor
For gene expression to occur, properly processed mRNA transcripts must be exported from the nucleus to the cytoplasm for translation of the information they encode. While many RNA binding proteins interact transiently with transcripts to mediate processing steps, others remain associated and regulate subsequent steps in post‐transcriptional gene expression. Studies in our laboratory provide insight into how one mRNA binding protein couples mRNA processing and export. The essential yeast Nab2 protein is an evolutionarily conserved zinc finger protein required both for proper polyadenylation and mRNA export. Our recent work reveals that Nab2 binds specifically to polyadenosine RNA through a novel zinc finger‐dependent mechanism. The conserved N‐terminal domain of Nab2, which assumes a PWI‐fold found in other mRNA binding proteins, then mediates interactions with Mlp1 located at the inner nuclear basket of the nuclear pore. Our recent resolution of the structure of the Nab2 N‐terminal domain allowed us to design and exploit Nab2 mutants to demonstrate that interaction between Nab2 and Mlp1 is important for proper mRNA export. Supported by a grant from the NIH.