Evolutionarily conserved cysteines in plant cytosolic seryl‐<scp>tRNA</scp> synthetase are important for its resistance to oxidation

Evic, Valentina; Soic, Ruzica; Mocibob, Marko; Kekez, Mario; Houser, Josef; Wimmerová, Michaela; Matković‐Čalogović, Dubravka; Gruic‐Sovulj, Ita; Kekez, Ivana; Rokov‐Plavec, Jasmina

doi:10.1002/1873-3468.14748

Cited by 2 publications

(4 citation statements)

References 83 publications

(118 reference statements)

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“…The cysteines involved in the disulfide bond in A. thaliana SerRS are evolutionarily conserved in all green plants. In oxidizing conditions, the formation of a disulfide link did not abolish the activity of plant SerRS, compared to the severely impaired activity of cysteine-to-serine mutants, which may be beneficial for translation during oxidative stress conditions in plants [68].…”

Section: Seryl-trna Synthetasesmentioning

confidence: 82%

“…compared to the severely impaired activity of cysteine-to-serine mutants, which may be beneficial for translation during oxidative stress conditions in plants [68].…”

Section: Seryl-trna Synthetasesmentioning

confidence: 99%

“…Thus, the partnership between SerRS and BEN1 signifies a link between the translation and steroid metabolic pathways within the plant cell. Although Arabidopsis SerRS gene expression was not modified during abiotic stress [130], it was shown that the disulfide link protects proteins against oxidative conditions [68] and that SerRS protein level is increased during cadmium exposure [131]. Considering that brassinosteroid hormones regulate plant stress response, SerRS:BEN1 interaction may be important in plant response mechanisms to changing environmental conditions, such as exposure to stressors [67].…”

Section: Arabidopsis Cytosolic Serrs and Ben1 Indicate A Link Between...mentioning

confidence: 99%

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Protein–Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease

Dulic,

Godinic-Mikulcic,

Kekez

et al. 2024

Life

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Seryl-tRNA synthetases (SerRSs), members of the aminoacyl-tRNA synthetase family, interact with diverse proteins, enabling SerRSs to enhance their role in the translation of the genetic message or to perform alternative functions in cellular processes beyond translation. Atypical archaeal SerRS interacts with arginyl-tRNA synthetase and proteins of the ribosomal P-stalk to optimize translation through tRNA channeling. The complex between yeast SerRS and peroxin Pex21p provides a connection between translation and peroxisome function. The partnership between Arabidopsis SerRS and BEN1 indicates a link between translation and brassinosteroid metabolism and may be relevant in plant stress response mechanisms. In Drosophila, the unusual heterodimeric mitochondrial SerRS coordinates mitochondrial translation and replication via interaction with LON protease. Evolutionarily conserved interactions of yeast and human SerRSs with m3C32 tRNA methyltransferases indicate coordination between tRNA modification and aminoacylation in the cytosol and mitochondria. Human cytosolic SerRS is a cellular hub protein connecting translation to vascular development, angiogenesis, lipogenesis, and telomere maintenance. When translocated to the nucleus, SerRS acts as a master negative regulator of VEGFA gene expression. SerRS alone or in complex with YY1 and SIRT2 competes with activating transcription factors NFκB1 and c-Myc, resulting in balanced VEGFA expression important for proper vascular development and angiogenesis. In hypoxia, SerRS phosphorylation diminishes its binding to the VEGFA promoter, while the lack of nutrients triggers SerRS glycosylation, reducing its nuclear localization. Additionally, SerRS binds telomeric DNA and cooperates with the shelterin protein POT1 to regulate telomere length and cellular senescence. As an antitumor and antiangiogenic factor, human cytosolic SerRS appears to be a promising drug target and therapeutic agent for treating cancer, cardiovascular diseases, and possibly obesity and aging.

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Section: Seryl-trna Synthetasesmentioning

confidence: 82%

“…compared to the severely impaired activity of cysteine-to-serine mutants, which may be beneficial for translation during oxidative stress conditions in plants [68].…”

Section: Seryl-trna Synthetasesmentioning

confidence: 99%

Section: Arabidopsis Cytosolic Serrs and Ben1 Indicate A Link Between...mentioning

confidence: 99%

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Protein–Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease

Dulic,

Godinic-Mikulcic,

Kekez

et al. 2024

Life

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“…It also has diverse effects on the aaRS function. In most cases it impairs the aaRS activity ( 36 , 37 , 38 , 39 ), but some aaRSs are resistant to oxidative conditions ( 40 , 41 , 42 , 43 ).…”

mentioning

confidence: 99%

Interplay between mistranslation and oxidative stress in Escherichia coli

Ević,

Rokov-Plavec

2024

Archives of Industrial Hygiene and Toxicology

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Mistakes in translation are mostly associated with toxic effects in the cell due to the production of functionally aberrant and misfolded proteins. However, under certain circumstances mistranslation can have beneficial effects and enable cells to preadapt to other stress conditions. Mistranslation may be caused by mistakes made by aminoacyl-tRNA synthetases, essential enzymes that link amino acids to cognate tRNAs. There is an Escherichia coli strain expressing isoleucyl-tRNA synthetase mutant variant with inactivated editing domain which produces mistranslated proteomes where valine (Val) and norvaline (Nva) are misincorporated into proteins instead of isoleucine. We compared this strain with the wild-type to determine the effects of such mistranslation on bacterial growth in oxidative stress conditions. When the cells were pre-incubated with 0.75 mmol/L Nva or 1.5 mmol/L Val or Nva and exposed to hydrogen peroxide, no beneficial effect of mistranslation was observed. However, when the editing-deficient strain was cultivated in medium supplemented with 0.75 mmol/L Val up to the early or mid-exponential phase of growth and then exposed to oxidative stress, it slightly outgrew the wild-type grown in the same conditions. Our results therefore show a modest adaptive effect of isoleucine mistranslation on bacterial growth in oxidative stress, but only in specific conditions. This points to a delicate balance between deleterious and beneficial effects of mistranslation.

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Evolutionarily conserved cysteines in plant cytosolic seryl‐tRNA synthetase are important for its resistance to oxidation

Cited by 2 publications

References 83 publications

Protein–Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease

Protein–Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease

Interplay between mistranslation and oxidative stress in Escherichia coli

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