TY  - JOUR
A1  - Montacié, Charlotte
A1  - Durut, Nathalie
A1  - Opsomer, Alison
A1  - Palm, Denise
A1  - Comella, Pascale
A1  - Picart, Claire
A1  - Carpentier, Marie-Christine
A1  - Pontvianne, Frederic
A1  - Carapito, Christine
A1  - Schleiff, Enrico
A1  - Sáez-Vásquez, Julio
T1  - Nucleolar proteome analysis and proteasomal activity assays reveal a link between nucleolus and 26S proteasome in A. thaliana
T2  - Frontiers in plant science
N2  - In all eukaryotic cells, the nucleolus is functionally and structurally linked to rRNA synthesis and ribosome biogenesis. This compartment contains as well factors involved in other cellular activities, but the functional interconnection between non-ribosomal activities and the nucleolus (structure and function) still remains an open question. Here, we report a novel mass spectrometry analysis of isolated nucleoli from Arabidopsis thaliana plants using the FANoS (Fluorescence Assisted Nucleolus Sorting) strategy. We identified many ribosome biogenesis factors (RBF) and proteins non-related with ribosome biogenesis, in agreement with the recognized multi-functionality of the nucleolus. Interestingly, we found that 26S proteasome subunits localize in the nucleolus and demonstrated that proteasome activity and nucleolus organization are intimately linked to each other. Proteasome subunits form discrete foci in the disorganized nucleolus of nuc1.2 plants. Nuc1.2 protein extracts display reduced proteasome activity in vitro compared to WT protein extracts. Remarkably, proteasome activity in nuc1.2 is similar to proteasome activity in WT plants treated with proteasome inhibitors (MG132 or ALLN). Finally, we show that MG132 treatment induces disruption of nucleolar structures in WT but not in nuc1.2 plants. Altogether, our data suggest a functional interconnection between nucleolus structure and proteasome activity.
KW  - proteasome
KW  - nucleolus
KW  - Arabidopsis
KW  - nucleolin
KW  - FANoS
Y1  - 2017
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/51542
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-515421
SN  - 1664-462X
N1  - Copyright: © 2017 Montacié, Durut, Opsomer, Palm, Comella, Picart, Carpentier, Pontvianne, Carapito, Schleiff and Sáez-Vásquez. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
VL  - 8
IS  - Art. 1815
SP  - 1
EP  - 13
PB  - Frontiers Media
CY  - Lausanne
ER  -