Structural and Biochemical Insights into the Multiple Functions of Yeast Grx3

Chi, Chongwei; Tang, Yajun; Zhang, Jiahai; Dai, Ya-Nan; Abdalla, Mohnad; Chen, Yuxing; Zhou, Cong‐Zhao

doi:10.1016/j.jmb.2018.02.024

Cited by 20 publications

(17 citation statements)

References 48 publications

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“…This indicates that changes in the secondary structure contents of the proteins occur upon complex formation. The protein regions and residues cannot be precisely mapped here but previous NMR studies have already shown that interfacing residues do not involve Fe-S cluster ligands [18][19][20][21][22]. As already determined, almost all interfacing residues are in β2/β3-strands and in α3-helix on the BolA side.…”

Section: Smyrba Interacts With Smgrx2mentioning

confidence: 79%

“…The study of the biochemical and structural properties of class II Grx and BolA recombinant proteins alone or in complex, showed that both Grx homodimers and Grx-BolA heterodimers bridged [2Fe-2S] clusters and that incubating BolAs with [2Fe-2S]-bridged Grx homodimers promoted their conversions into more stable [2Fe-2S]-bridged BolA-Grx heterodimers [11][12][13][14][15][16][17][18][19]. Using NMR spectroscopy, it was revealed that Grx and BolA form both apo-and holo-complexes and that the structure of such complexes is primarily driven by electrostatic interactions, involving a putative DNA-binding region in BolAs which adopts a helix-turn-helix structure resembling the one found in K-homology domain proteins [18][19][20][21][22]. For the ligation of the Fe-S clusters in holo-heterodimers, the Grx partner provides cysteine ligands, one from the polypeptide and one from a bound glutathione, whereas the BolA partner provides a histidine ligand, a residue that is totally conserved in the family, and either a second histidine or a cysteine, located in the loop connecting the two first β-strands that was named the [H/C]-loop [13,18,23].…”

Section: Introductionmentioning

confidence: 99%

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Sinorhizobium melilotiYrbA binds divalent metal cations using two conserved histidines

et al. 2020

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Sinorhizobium meliloti is a nitrogen-fixing bacterium forming symbiotic nodules with the legume Medicago truncatula. S. meliloti possesses two BolA-like proteins (BolA and YrbA), the function of which is unknown. In organisms where BolA proteins and monothiol glutaredoxins (Grxs) are present, they contribute to the regulation of iron homeostasis by bridging a [2Fe-2S] cluster into heterodimers. A role in the maturation of iron-sulfur (Fe-S) proteins is also attributed to both proteins. In this study, we have performed a structure-function analysis of SmYrbA showing that it coordinates diverse divalent metal ions (Fe2+, Co2+, Ni2+, Cu2+ and Zn2+) using His32 and His67 residues, that are also used for Fe-S cluster binding in BolA-Grx heterodimers. It also possesses the capacity to form heterodimers with the sole monothiol glutaredoxin (SmGrx2) present in this species. Using cellular approaches analyzing the metal tolerance of S. meliloti mutant strains inactivated in the yrbA and/or bolA genes, we provide evidence for a connection of YrbA with the regulation of iron homeostasis. The mild defects in M. truncatula nodulation reported for the yrbAbolA mutant as compared to the stronger defects in nodule development previously observed for a grx2 mutant suggest functions independent of SmGrx2. These results help clarifying the physiological role of BolA-type proteins in bacteria.

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Section: Smyrba Interacts With Smgrx2mentioning

confidence: 79%

Section: Introductionmentioning

confidence: 99%

Sinorhizobium melilotiYrbA binds divalent metal cations using two conserved histidines

et al. 2020

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“…In S. cerevisiae , the cytosolic monothiol glutaredoxins Grx3 and Grx4 play a central role in communicating the mitochondrial iron status to Aft1 and Aft2 ( Ojeda et al, 2006 ; Pujol-Carrion et al, 2006 ; Kumanovics et al, 2008 ). In iron replete cells, the mitochondrial Fe–S clusters biogenesis is very active and Fe–S clusters are exported to the cytosol where Grx3 and Grx4 form Fe–S bridged homodimers which has the capacity to transfer its Fe–S cluster to Aft1 and Aft2, therefore decreasing their DNA binding affinity by favoring the formation of Fe/S bridged Aft homodimers ( Kumanovics et al, 2008 ; Ueta et al, 2012 ; Poor et al, 2014 ; Chi et al, 2018 ). This role of Grx3/4 proteins in the regulation of iron homeostasis is conserved from yeasts to humans ( Li et al, 2012 ; Labbe et al, 2013 ; Jacques et al, 2014 ; Banci et al, 2015 ; Encinar del Dedo et al, 2015 ).…”

Section: Discussionmentioning

confidence: 99%

Comparative Transcriptomics Highlights New Features of the Iron Starvation Response in the Human Pathogen Candida glabrata

et al. 2018

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In this work, we used comparative transcriptomics to identify regulatory outliers (ROs) in the human pathogen Candida glabrata. ROs are genes that have very different expression patterns compared to their orthologs in other species. From comparative transcriptome analyses of the response of eight yeast species to toxic doses of selenite, a pleiotropic stress inducer, we identified 38 ROs in C. glabrata. Using transcriptome analyses of C. glabrata response to five different stresses, we pointed out five ROs which were more particularly responsive to iron starvation, a process which is very important for C. glabrata virulence. Global chromatin Immunoprecipitation and gene profiling analyses showed that four of these genes are actually new targets of the iron starvation responsive Aft2 transcription factor in C. glabrata. Two of them (HBS1 and DOM34b) are required for C. glabrata optimal growth in iron limited conditions. In S. cerevisiae, the orthologs of these two genes are involved in ribosome rescue by the NO GO decay (NGD) pathway. Hence, our results suggest a specific contribution of NGD co-factors to the C. glabrata adaptation to iron starvation.

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“…The crystal structures of yeast Grx1, Grx2, Grx5, Grx6, and Grx8 have been solved and their enzymatic activities compared. These analyses showed the diversity of Grxs which are encoded by the same organism from both catalytic and structural points of view [13–16]. …”

Section: Introductionmentioning

confidence: 99%

Comparison of structures among Saccharomyces cerevisiae Grxs proteins

2018

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Glutaredoxins (Grxs) comprise a group of glutathione (GSH)-dependent oxidoreductase enzymes that respond to oxidative stress and sustain redox homeostasis. Saccharomyces cerevisiae Grx has a similar interaction patterns through its residues between the residues and the environment. The glutaredoxin domain covers 100% of the entire mature Grx1 and Grx8, while the glutaredoxin domain covers ~ 52% of the entire mature Grx6 and Grx7, which have approximately 74 additional amino acids in their N-terminal regions, whereas Grx3 and Grx4 have two functional domains: glutaredoxin and thioredoxin. We have presented the prediction of disordered regions within these protein sequences. Multiple sequence alignment combined with a phylogenetic tree enabled us to specify the key residues contributing to the differences between Saccharomyces cerevisiae Grxs and the proportion symmetry.

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Structural and Biochemical Insights into the Multiple Functions of Yeast Grx3

Cited by 20 publications

References 48 publications

Sinorhizobium melilotiYrbA binds divalent metal cations using two conserved histidines

Sinorhizobium melilotiYrbA binds divalent metal cations using two conserved histidines

Comparative Transcriptomics Highlights New Features of the Iron Starvation Response in the Human Pathogen Candida glabrata

Comparison of structures among Saccharomyces cerevisiae Grxs proteins

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