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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/49437
Title: Nab2 functions in the metabolism of RNA driven by polymerases II and III
Authors: González-Aguilera, Cristina; Tous, Cristina; Babiano, Reyes; Cruz, Jesús de la; Luna, Rosa; Aguilera, Andrés
Keywords: Nab2 protein
Nucleocytoplasmic transport proteins
Saccharomyces cerevisiae proteins
Poly A
RNA polymerase II
RNA polymerase III
Cell nucleus
Issue Date: 1-Aug-2011
Publisher: American Society for Cell Biology
Citation: Molecular Biology of the Cell 22(15): 2729-2740 (2011)
Abstract: Gene expression in eukaryotes is an essential process that includes transcription, RNA processing, and export. One important player in this interface is the poly(A)+-RNA–binding protein Nab2, which regulates the mRNA poly(A)+-tail length and export. Here we show that Nab2 has additional roles during mRNA transcription, tRNA metabolism, and ribosomal subunit export. Nab2 is associated with the entire open reading frame of actively transcribed RNA polymerase (RNAP) II and III genes. As a consequence, nab2 mutations confer translation defects that are detected by polysome profiling. Genome-wide analysis of expression of a conditional degron nab2 mutant shows that the role of Nab2 in RNAPII transcription and RNAPIII metabolism is direct. Taken together, our results identify novel functions for Nab2 in transcription and metabolism of most types of RNAs, indicating that Nab2 function is more ubiquitous than previously anticipated, and that it is a central player in the general and coordinated control of gene expression from transcription to translation.
Description: This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License.
Publisher version (URL): http://dx.doi.org/10.1091/mbc.E11-01-0055
URI: http://hdl.handle.net/10261/49437
DOI: 10.1091/mbc.E11-01-0055
ISSN: 1059-1524
E-ISSN: 1939-4586
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