Universität zu Köln

Moseler, Anna ORCID: 0000-0003-4641-8093, Kruse, Inga ORCID: 0000-0003-1935-1647, Maclean, Andrew E., Pedroletti, Luca ORCID: 0000-0002-8594-1306, Franceschetti, Marina, Wagner, Stephan ORCID: 0000-0001-5369-7911, Wehler, Regina, Fischer-Schrader, Katrin ORCID: 0000-0003-4532-8918, Poschet, Gernot, Wirtz, Markus ORCID: 0000-0001-7790-4022, Doermann, Peter, Hildebrandt, Tatjana M., Hell, Ruediger, Schwaerzlaender, Markus, Balk, Janneke and Meyer, Andreas J. (2021). The function of glutaredoxin GRXS15 is required for lipoyl-dependent dehydrogenases in mitochondria. Plant Physiol., 186 (3). S. 1507 - 1526. CARY: OXFORD UNIV PRESS INC. ISSN 1532-2548

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Abstract

Iron-sulfur (Fe-S) clusters are ubiquitous cofactors in all life and are used in a wide array of diverse biological processes, including electron transfer chains and several metabolic pathways. Biosynthesis machineries for Fe-S clusters exist in plastids, the cytosol, and mitochondria. A single monothiol glutaredoxin (GRX) is involved in Fe-S cluster assembly in mitochondria of yeast and mammals. In plants, the role of the mitochondrial homolog GRXS15 has only partially been characterized. Arabidopsis (Arabidopsis thaliana) grxs15 null mutants are not viable, but mutants complemented with the variant GRXS15 K83A develop with a dwarf phenotype similar to the knockdown line GRXS15(amiR). In an in-depth metabolic analysis of the variant and knockdown GRXS15 lines, we show that most Fe-S cluster-dependent processes are not affected, including biotin biosynthesis, molybdenum cofactor biosynthesis, the electron transport chain, and aconitase in the tricarboxylic acid (TCA) cycle. Instead, we observed an increase in most TCA cycle intermediates and amino acids, especially pyruvate, glycine, and branched-chain amino acids (BCAAs). Additionally, we found an accumulation of branched-chain alpha-keto acids (BCKAs), the first degradation products resulting from transamination of BCAAs. In wild-type plants, pyruvate, glycine, and BCKAs are all metabolized through decarboxylation by mitochondrial lipoyl cofactor (LC)-dependent dehydrogenase complexes. These enzyme complexes are very abundant, comprising a major sink for LC. Because biosynthesis of LC depends on continuous Fe-S cluster supply to lipoyl synthase, this could explain why LC-dependent processes are most sensitive to restricted Fe-S supply in grxs15 mutants.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Moseler, Anna UNSPECIFIED orcid.org/0000-0003-4641-8093 UNSPECIFIED Kruse, Inga UNSPECIFIED orcid.org/0000-0003-1935-1647 UNSPECIFIED Maclean, Andrew E. UNSPECIFIED UNSPECIFIED UNSPECIFIED Pedroletti, Luca UNSPECIFIED orcid.org/0000-0002-8594-1306 UNSPECIFIED Franceschetti, Marina UNSPECIFIED UNSPECIFIED UNSPECIFIED Wagner, Stephan UNSPECIFIED orcid.org/0000-0001-5369-7911 UNSPECIFIED Wehler, Regina UNSPECIFIED UNSPECIFIED UNSPECIFIED Fischer-Schrader, Katrin UNSPECIFIED orcid.org/0000-0003-4532-8918 UNSPECIFIED Poschet, Gernot UNSPECIFIED UNSPECIFIED UNSPECIFIED Wirtz, Markus UNSPECIFIED orcid.org/0000-0001-7790-4022 UNSPECIFIED Doermann, Peter UNSPECIFIED UNSPECIFIED UNSPECIFIED Hildebrandt, Tatjana M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Hell, Ruediger UNSPECIFIED UNSPECIFIED UNSPECIFIED Schwaerzlaender, Markus UNSPECIFIED UNSPECIFIED UNSPECIFIED Balk, Janneke UNSPECIFIED UNSPECIFIED UNSPECIFIED Meyer, Andreas J. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-602472
DOI:	10.1093/plphys/kiab172
Journal or Publication Title:	Plant Physiol.
Volume:	186
Number:	3
Page Range:	S. 1507 - 1526
Date:	2021
Publisher:	OXFORD UNIV PRESS INC
Place of Publication:	CARY
ISSN:	1532-2548
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language AMINO-ACID CATABOLISM; ELECTRON-TRANSPORT CHAIN; IRON-SULFUR CLUSTER; ARABIDOPSIS-THALIANA; SUCCINATE-DEHYDROGENASE; MONOTHIOL GLUTAREDOXIN; GENE-EXPRESSION; PLANT-CELLS; COMPLEX I; MUTANT Multiple languages Plant Sciences Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/60247