Arabidopsis Glutaredoxin S17 and Its Partner, the Nuclear Factor Y Subunit C11/Negative Cofactor 2α, Contribute to Maintenance of the Shoot Apical Meristem under Long-Day Photoperiod

Knuesting, Johannes; Riondet, Christophe; Carlos, María; Kruse, Inga; Bécuwe, Noëlle; König, Nicolas; Berndt, Carsten; Tourrette, Sébastien; Guilleminot-Montoya, Jocelyne; Herrero, Enrique; Gaymard, Frédéric; Balk, Janneke; Bellı́, Gemma; Scheibe, Renate; Reichheld, Jean‐Philippe; Rouhier, Nicolas; Rey, Pascal

doi:10.1104/pp.15.00049

Cited by 81 publications

(85 citation statements)

References 80 publications

(99 reference statements)

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“…2B). Hence, similar to what was previously found for the enzymes cytosolic aconitase and aldehyde oxidase (Knuesting et al, 2015), our findings indicate that GRXS17 is not essential for XDH1 enzyme activity in plants.…”

Section: Metabolic Profiling Of Loss-of-function Grxs17 Plants Pointssupporting

confidence: 76%

“…Although human and yeast GRXS17 orthologs are essential for the maturation of cytosolic and nuclear Fe-S proteins (Mühlenhoff et al, 2010;Haunhorst et al, 2013), Arabidopsis GRXS17 has recently been shown to play only a minor role in maintaining the activity of two classes of cytosolic Fe-S enzymes (aconitases and aldehyde oxidases; Knuesting et al, 2015). Nonetheless, we identified another Fe-S enzyme, XDH1, to be associated with GRXS17 (Table I).…”

Section: Metabolic Profiling Of Loss-of-function Grxs17 Plants Pointsmentioning

confidence: 68%

“…A transfer DNA (T-DNA) insertion line (grxs17-1; SALK_021301) described previously (Supplemental Fig. S1; Cheng et al, 2011;Knuesting et al, 2015) was characterized in detail and found to lack both GRXS17 transcripts (Supplemental Fig. S2B) and GRXS17 protein (Supplemental Fig.…”

Section: Grxs17 Associates With the Cia Complex And Fe-s Proteinsmentioning

confidence: 99%

“…GRXS17 dimers are capable of associating with three [2Fe-2S] clusters in vitro (Knuesting et al, 2015). Its physiological and molecular role in plants is not well understood (Couturier et al, 2013).…”

mentioning

confidence: 99%

“…Its physiological and molecular role in plants is not well understood (Couturier et al, 2013). GRXS17 function has been associated with protection against oxidative stress in Arabidopsis and thermotolerance in Arabidopsis and tomato (Cheng et al, 2011;Wu et al, 2012;Knuesting et al, 2015). Arabidopsis GRXS17 loss-of-function plants (grxs17) are hypersensitive to heat stress and show alterations in auxin sensitivity and polar transport (Cheng et al, 2011).…”

mentioning

confidence: 99%

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Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway

et al. 2016

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Cytosolic monothiol glutaredoxins (GRXs) are required in iron-sulfur (Fe-S) cluster delivery and iron sensing in yeast and mammals. In plants, it is unclear whether they have similar functions. Arabidopsis (Arabidopsis thaliana) has a sole class II cytosolic monothiol GRX encoded by GRXS17. Here, we used tandem affinity purification to establish that Arabidopsis GRXS17 associates with most known cytosolic Fe-S assembly (CIA) components. Similar to mutant plants with defective CIA components, grxs17 loss-of-function mutants showed some degree of hypersensitivity to DNA damage and elevated expression of DNA damage marker genes. We also found that several putative Fe-S client proteins directly bind to GRXS17, such as XANTHINE DEHYDROGENASE1 (XDH1), involved in the purine salvage pathway, and CYTOSOLIC THIOURIDYLASE SUBUNIT1 and CYTOSOLIC THIOURIDYLASE SUBUNIT2, both essential for the 2-thiolation step of 5-methoxycarbonylmethyl-2-thiouridine (mcm 5 s 2 U) modification of tRNAs. Correspondingly, profiling of the grxs17-1 mutant pointed to a perturbed flux through the purine degradation pathway and revealed that it phenocopied mutants in the elongator subunit ELO3, essential for the mcm 5 tRNA modification step, although we did not find XDH1 activity or tRNA thiolation to be markedly reduced in the grxs17-1 mutant. Taken together, our data suggest that plant cytosolic monothiol GRXs associate with the CIA complex, as in other eukaryotes, and contribute to, but are not essential for, the correct functioning of client Fe-S proteins in unchallenged conditions.

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Section: Metabolic Profiling Of Loss-of-function Grxs17 Plants Pointssupporting

confidence: 76%

Section: Metabolic Profiling Of Loss-of-function Grxs17 Plants Pointsmentioning

confidence: 68%

Section: Grxs17 Associates With the Cia Complex And Fe-s Proteinsmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway

et al. 2016

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FeSCluster Assembly: Role of MonothiolGrxsandNfuProteins

Przybyla-Toscano

Roret

Couturier

et al. 2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

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The cellular maturation of iron–sulfur (Fe–S) proteins necessitates dedicated assembly machineries. In eukaryotes, the ISC (iron–sulfur cluster) and SUF (sulfur mobilization) machineries are autonomous biogenesis systems for mitochondrial and chloroplastic proteins respectively, whereas the cytosolic CIA (cytosolic iron–sulfur cluster assembly) machinery operates for cytosolic and nuclear proteins and depends on the ISC machinery for obtaining the required labile sulfur atoms. Owing to their capacity to incorporate Fe–S clusters alone or in complex with BOLA proteins, class II glutaredoxins (GRXs) play some key roles in this maturation process, although the precise roles have yet to be clearly delineated. Organellar GRXs likely serve as Fe–S transfer proteins, accepting preformed Fe–S clusters from scaffold proteins used for their de novo synthesis before delivering them to other ISC or SUF targeting factors such as ISCA proteins or to final client proteins. The cytosolic/nuclear localized GRXs seem to have at least three different crucial roles, likely originating from their key position connecting the ISC machinery to the cytosolic compartment. Indeed, the molecular analysis of yeast mutants suggests that it could be the primary recipient protein of the unknown sulfur compound exported from the mitochondria and which could serve to assemble its Fe–S cluster. The presence of the cluster seems mandatory for all identified functions, serving (i) for the maturation of Fe–S clusters in the CIA electron donor DRE2, (ii) for the regulation of iron homeostasis in conjunction with BOLA and the Aft1/2 transcriptional regulators, and (iii) for the proper distribution of iron and correct functioning of all iron‐dependent proteins. These roles might not all be evolutionary conserved, notably in plants. In addition to providing an overview of the known physiological roles of class II GRXs, we describe their biochemical and structural properties focusing in particular on their interaction with other maturation factors of the BOLA, DRE2, and ISCA families.

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Cloning and functional analysis of LH2, a gene controlling late heading in rice

et al. 2021

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Heading date is an important agronomic trait in rice (Oryza sativa L.). We previously fine-mapped two complementary genes, Late Heading Date 1 and Late Heading Date 2 (LH2), that control the late heading trait in rice. Here, we cloned and analyzed the function of LH2. LH2 was fine-mapped to a 53-kb genomic region. Sequencing analysis revealed that there were differences in the coding sequence of LOC_Os08g07740 between the varieties 'Bo B' and 'Yuefeng B'. Therefore, LOC_Os08g07740 was identified as a candidate gene for LH2 and subsequently determined that LH2 is a Type 3 allele of Days To Heading 8. Transgenic plants of Yuefeng B carrying LH2 from Bo B significantly delayed the heading date under short-day and long-day conditions. A yeast two-hybrid analysis revealed that LH2 physically interacted with Heme Activator Protein (HAP) 5A, -H, -I, -L, -K, and HAP5-LIKE. The HAP5 domain of HAP5 family members has various functions. Further analysis revealed that LH2 represses photoperiodic flowering by controlling the expression of Early Heading Date 1, Heading date 3a, and Rice Flowering Locus T1 in rice.

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Arabidopsis Glutaredoxin S17 and Its Partner, the Nuclear Factor Y Subunit C11/Negative Cofactor 2α, Contribute to Maintenance of the Shoot Apical Meristem under Long-Day Photoperiod

Cited by 81 publications

References 80 publications

Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway

Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway

FeSCluster Assembly: Role of MonothiolGrxsandNfuProteins

Cloning and functional analysis of LH2, a gene controlling late heading in rice

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