Fernando A Gonzales-Zubiate, Ellen K Okuda, Julia P C Da Cunha, Carla Columbano Oliveira
The Journal of biological chemistry 2017 Jul 21The exosome is a conserved multiprotein complex essential for RNA processing and degradation. The nuclear exosome is a key factor for pre-rRNA processing through the activity of its catalytic subunits, Rrp6 and Rrp44. In Saccharomyces cerevisiae, Rrp6 is exclusively nuclear and has been shown to interact with exosome cofactors. With the aim of analyzing proteins associated with the nuclear exosome, in this work, we purified the complex with Rrp6-TAP, identified the co-purified proteins by mass spectrometry, and found karyopherins to be one of the major groups of proteins enriched in the samples. By investigating the biological importance of these protein interactions, we identified Srp1, Kap95, and Sxm1 as the most important karyopherins for Rrp6 nuclear import and the nuclear localization signals recognized by them. Based on the results shown here, we propose a model of multiple pathways for the transport of Rrp6 to the nucleus. © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.
Fernando A Gonzales-Zubiate, Ellen K Okuda, Julia P C Da Cunha, Carla Columbano Oliveira. Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 in Saccharomyces cerevisiae. The Journal of biological chemistry. 2017 Jul 21;292(29):12267-12284
PMID: 28539363
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