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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Proteomic Analysis of Yeast Mutant RNA Exosome Complexes

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Author(s):
Lourenco, Rogerio F. [1] ; Leme, Adriana F. P. [2] ; Oliveira, Carla C. [1]
Total Authors: 3
Affiliation:
[1] Univ Sao Paulo, Inst Chem, Dept Biochem, BR-05508000 Sao Paulo - Brazil
[2] Brazilian Biosci Natl Lab CNPEM, Mass Spectrometry Lab, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: JOURNAL OF PROTEOME RESEARCH; v. 12, n. 12, p. 5912-5922, DEC 2013.
Web of Science Citations: 4
Abstract

The yeast exosome is a conserved multiprotein complex essential for RNA processing and degradation. The complex is formed by a nine-subunit core that associates with two hydrolytic 3'-5' exoribonucleases. Although catalytically inert, the assembly of this nine-subunit core seems to be essential for the exosome activity, as mutations in regions that do not directly bind RNA or are not in the active sites of the exonucleases impair the function of the complex. Previously isolated mutations in the exosome core subunit Rrp43p have been shown to negatively affect the function of the complex. With the aim of investigating the effect of these mutations on the complex stability and activity, Rrp43p and its mutant forms were purified by means of the TAP method. Mass spectrometry analyses showed that lower amounts of the exosome subunits are copurified with the mutant Rrp43p proteins. Additionally, by decreasing the stability of the exosome, other nonspecific protein interactions are favored (the data have been deposited to the ProteomeXchange with identifier PXD000580). Exosome copurified with mutant Rrp43p exhibited increased exonuclease activity, suggesting higher dissociation constants for these mutant complexes. Therefore, data reported here indicate that complexes containing a mutant Rrp43p exhibit decreased stability and provide information on additional protein interactions. (AU)

FAPESP's process: 10/51842-3 - Structural study of protein components of the exosome and some of its regulatory factors from Archaea and yeast
Grantee:Carla Columbano de Oliveira
Support Opportunities: Research Projects - Thematic Grants