SUMOlock reveals a more complete Aspergillus nidulans SUMOylome.
Aspergillus nidulans
SUMO
SUMOylated proteins
SUMOylation pathway
Journal
Fungal genetics and biology : FG & B
ISSN: 1096-0937
Titre abrégé: Fungal Genet Biol
Pays: United States
ID NLM: 9607601
Informations de publication
Date de publication:
06 2019
06 2019
Historique:
received:
08
02
2019
revised:
04
03
2019
accepted:
04
03
2019
pubmed:
9
3
2019
medline:
31
1
2020
entrez:
9
3
2019
Statut:
ppublish
Résumé
SUMOylation, covalent attachment of the small ubiquitin-like modifier protein SUMO to proteins, regulates protein interactions and activity and plays a crucial role in the regulation of many key cellular processes. Understanding the roles of SUMO in these processes ultimately requires identification of the proteins that are SUMOylated in the organism under study. The filamentous fungus Aspergillus nidulans serves as an excellent model for many aspects of fungal biology, and it would be of great value to determine the proteins that are SUMOylated in this organism (i.e. its SUMOylome). We have developed a new and effective approach for identifying SUMOylated proteins in this organism in which we lock proteins in their SUMOylated state, affinity purify SUMOylated proteins using the high affinity S-tag, and identify them using sensitive Orbitrap mass spectroscopy. This approach allows us to distinguish proteins that are SUMOylated from proteins that are binding partners of SUMOylated proteins or are bound non-covalently to SUMO. This approach has allowed us to identify 149 proteins that are SUMOylated in A. nidulans. Of these, 67 are predicted to be involved in transcription and particularly in the regulation of transcription, 21 are predicted to be involved in RNA processing and 16 are predicted to function in DNA replication or repair.
Identifiants
pubmed: 30849444
pii: S1087-1845(19)30042-8
doi: 10.1016/j.fgb.2019.03.002
pmc: PMC6673660
mid: NIHMS1524612
pii:
doi:
Substances chimiques
Fungal Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
50-59Subventions
Organisme : NIGMS NIH HHS
ID : P01 GM084077
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM031837
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM042564
Pays : United States
Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.
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