---
reference_id: PMID:27497447
title: The Arabidopsis Iron-Sulfur Protein GRXS17 is a Target of the Ubiquitin E3 Ligases RGLG3 and RGLG4.
authors:
- Nagels Durand A
- Iñigo S
- Ritter A
- Iniesto E
- De Clercq R
- Staes A
- Van Leene J
- Rubio V
- Gevaert K
- De Jaeger G
- Pauwels L
- Goossens A
journal: Plant Cell Physiol
year: '2016'
doi: 10.1093/pcp/pcw122
keywords:
- "Arabidopsis/genetics, metabolism"
- "Arabidopsis Proteins/genetics, metabolism"
- Cyclopentanes/metabolism
- "Glutaredoxins/genetics, metabolism"
- Iron-Sulfur Proteins/metabolism
- "Ligases/genetics, metabolism"
- Mutation
- Oxylipins/metabolism
- "Plants, Genetically Modified"
- Polyubiquitin/metabolism
- Proteasome Endopeptidase Complex/metabolism
- Signal Transduction
- Two-Hybrid System Techniques
- "Ubiquitin-Conjugating Enzymes/genetics, metabolism"
- Ubiquitination
content_type: abstract_only
full_text_attempted: true
---

# The Arabidopsis Iron-Sulfur Protein GRXS17 is a Target of the Ubiquitin E3 Ligases RGLG3 and RGLG4.
**Authors:** Nagels Durand A, Iñigo S, Ritter A, Iniesto E, De Clercq R, Staes A, Van Leene J, Rubio V, Gevaert K, De Jaeger G, Pauwels L, Goossens A
**Journal:** Plant Cell Physiol (2016)
**DOI:** [10.1093/pcp/pcw122](https://doi.org/10.1093/pcp/pcw122)

## Content

1. Plant Cell Physiol. 2016 Sep;57(9):1801-13. doi: 10.1093/pcp/pcw122. Epub 2016
 Aug 6.

The Arabidopsis Iron-Sulfur Protein GRXS17 is a Target of the Ubiquitin E3 
Ligases RGLG3 and RGLG4.

Nagels Durand A(1), Iñigo S(1), Ritter A(2), Iniesto E(3), De Clercq R(2), Staes 
A(4), Van Leene J(2), Rubio V(3), Gevaert K(4), De Jaeger G(2), Pauwels L(1), 
Goossens A(5).

Author information:
(1)Department of Plant Systems Biology, VIB, Technologiepark 927, B-9052 Gent, 
Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 
Technologiepark 927, B-9052 Gent, Belgium These authors contributed equally to 
this work.
(2)Department of Plant Systems Biology, VIB, Technologiepark 927, B-9052 Gent, 
Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 
Technologiepark 927, B-9052 Gent, Belgium.
(3)Plant Molecular Genetics Department, National Centre for Biotechnology (CNB), 
Consejo Superior de Investigaciones Científicas (CSIC), Campus Universidad 
Autónoma, Madrid, Spain.
(4)Medical Biotechnology Center, VIB, B-9000 Ghent, Belgium Department of 
Biochemistry, Ghent University, B-9000 Ghent, Belgium.
(5)Department of Plant Systems Biology, VIB, Technologiepark 927, B-9052 Gent, 
Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 
Technologiepark 927, B-9052 Gent, Belgium These authors contributed equally to 
this work. algoo@psb.vib-ugent.be.

The stability of signaling proteins in eukaryotes is often controlled by 
post-translational modifiers. For polyubiquitination, specificity is assured by 
E3 ubiquitin ligases. Although plant genomes encode hundreds of E3 ligases, only 
few targets are known, even in the model Arabidopsis thaliana. Here, we 
identified the monothiol glutaredoxin GRXS17 as a substrate of the Arabidopsis 
E3 ubiquitin ligases RING DOMAIN LIGASE 3 (RGLG3) and RGLG4 using a substrate 
trapping approach involving tandem affinity purification of RING-dead versions. 
Simultaneously, we used a ubiquitin-conjugating enzym (UBC) panel screen to 
pinpoint UBC30 as a cognate E2 UBC capable of interacting with RGLG3 and RGLG4 
and mediating auto-ubiquitination of RGLG3 and ubiquitination of GRXS17 in 
vitro. Accordingly, GRXS17 is ubiquitinated and degraded in an RGLG3- and 
RGLG4-dependent manner in planta. The truncated hemoglobin GLB3 also interacted 
with RGLG3 and RGLG4 but appeared to obstruct RGLG3 ubiquitination activity 
rather than being its substrate. Our results suggest that the RGLG family is 
intimately linked to the essential element iron.

© The Author 2016. Published by Oxford University Press on behalf of Japanese 
Society of Plant Physiologists. All rights reserved. For permissions, please 
email: journals.permissions@oup.com.

DOI: 10.1093/pcp/pcw122
PMID: 27497447 [Indexed for MEDLINE]