Substrate recognition and fidelity of maize seryl-tRNA synthetases

Rokov-Plavec, Jasmina; Lesjak, Sonja; Gruić-Sovulj, Ita; Močibob, Marko; Dulić, Morana; Weygand-Đurašević, Ivana

doi:10.1016/j.abb.2012.11.014

Cited by 12 publications

(16 citation statements)

References 71 publications

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“…By using in vitro experiments it has been shown that the atypical methanogenic-type archaeal SerRS recognizes tRNAs Ser from all three domains of life, probably due to the fact that archaeal tRNAs Ser show mixed bacterial and eukaryotic features. [84,89] However, this SerRS was unable to complement the function of bacterial and yeast SerRSs in vivo. [90] Recently we demonstrated that the maize cytosolic SerRS can efficiently aminoacylate in vitro and in vivo bacterial tRNAs Ser [67] and eukaryotic cytosolic tRNAs Ser .…”

Section: Specific Features Of Trna Recognition and Aminoacylationmentioning

confidence: 99%

“…Length and orientation of the variable arm were shown to be important for proper recognition of tRNA Ser by SerRS enzymes and they differ among three domains of life. [82][83][84][85] Cross-species recognition of the tRNA Ser determined from in vitro aminoacylation and in vivo complementation assays is shown in Table 1.…”

Section: Specific Features Of Trna Recognition and Aminoacylationmentioning

confidence: 99%

“…[66] Thus, one of them should be dually targeted to account for the SerRS function needed in three protein synthesizing compartments. One of the identified maize SerRS proteins is targeted exclusively to maize cytosol [67] (Figure 3), aminoacylates yeast and maize cytosolic tRNAs Ser and complements the function of the yeast cytosolic SerRS. [68] The other SerRS protein complements the function of the E. coli SerRS [69] and aminoacylates efficiently mitochondrial and chloroplasts tRNAs Ser , [70] indicating its organellar function.…”

Section: Localization In Maize and Arabidopsis Thalianamentioning

confidence: 99%

“…[90] Recently we demonstrated that the maize cytosolic SerRS can efficiently aminoacylate in vitro and in vivo bacterial tRNAs Ser [67] and eukaryotic cytosolic tRNAs Ser . [67,68] Thus, despite its eukaryotic features and strong similarity to other eukaryotic cytosolic SerRSs, [70] the maize cytosolic SerRS was able to efficiently recognize bacterial tRNAs Ser that are clearly distinguishable from maize cytosolic tRNAs Ser , which show typical eukaryotic characteristics, [67,84] Similar broad tRNAs Ser specificity and flexibility was also shown for Arabidopsis cytosolic SerRS. [75] Broad tRNA Ser specificity may be related to the evolutionary origin of plant SerRSs.…”

Section: Specific Features Of Trna Recognition and Aminoacylationmentioning

confidence: 99%

“…Proofreading activities were shown for only few plant aaRSs. [92][93][94] Findings that yeast and archaeal SerRSs showed low or moderate misactivation of near-cognate amino acids and serine analogue SerHX [28,55,95] prompted us to explore the fidelity of the maize cytosolic and dually targeted organellar SerRSs, [67] Organellar SerRS exhibited higher discrimination against threonine, cysteine and SerHX as compared to its cytosolic counterpart. Both enzymes showed pre-transfer editing activity towards tested compounds implying their high overall accuracy.…”

Section: Fidelity Of Serylation In Plantsmentioning

confidence: 99%

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Seryl-tRNA Synthetases in Translation and Beyond

Močibob¹,

Rokov-Plavec²,

Godinić-Mikulčić³

et al. 2016

Croat. Chem. Acta

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Abstract:For a long time seryl-tRNA synthetases (SerRSs) stood as an archetypal, canonical aminoacyl-tRNA synthetases (aaRS), exhibiting only basic tRNA aminoacylation activity and with no moonlighting functions beyond protein biosynthesis. The picture has changed substantially in recent years after the discovery that SerRSs play an important role in antibiotic production and resistance and act as a regulatory factor in vascular development, as well as after the discovery of mitochondrial morphogenesis factor homologous to SerRS in insects. In this review we summarize the recent research results from our laboratory, which advance the understanding of seryl-tRNA synthetases and further paint the dynamic picture of unexpected SerRS activities. SerRS from archaeon Methanothermobacter thermautotrophicus was shown to interact with the large ribosomal subunit and it was postulated to contribute to a more efficient translation by the"tRNA channeling" hypothesis. Discovery of the atypical SerRS in a small number of methanogenic archaea led to the discovery of a new family of enzymes in numerous bacteria -amino acid:[carrier protein] ligases (aa:CP ligases). These SerRS homologues resigned tRNA aminoacylation activity, and instead adopted carrier proteins as the acceptors of activated amino acids. The crystal structure of the aa:CP ligase complex with the carrier protein revealed that the interactions between two macromolecules are incomparable to tRNA binding by the aaRS and consequently represent a true evolutionary invention. Kinetic investigations of SerRSs and the accuracy of amino acid selection revealed that SerRSs possess pre-transfer proofreading activity, challenging the widely accepted presumption that hydrolytic proofreading activity must reside in an additional, separate editing domain, not present in SerRSs. Finally, the plant tRNA serylation system is discussed, which is particularly interesting due to the fact that protein biosynthesis takes place in three cellular compartments: cytosol, mitochondria and chloroplasts. Plant cytosolic SerRSs showed broad tRNA Ser specificity and flexibility, unlike SerRSs from other organisms. High fidelity of SerRS dually targeted to mitochondria and chloroplasts indicated its importance in plant organellar quality control.

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Section: Specific Features Of Trna Recognition and Aminoacylationmentioning

confidence: 99%

Section: Specific Features Of Trna Recognition and Aminoacylationmentioning

confidence: 99%

Section: Localization In Maize and Arabidopsis Thalianamentioning

confidence: 99%

Section: Specific Features Of Trna Recognition and Aminoacylationmentioning

confidence: 99%

Section: Fidelity Of Serylation In Plantsmentioning

confidence: 99%

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Seryl-tRNA Synthetases in Translation and Beyond

Močibob¹,

Rokov-Plavec²,

Godinić-Mikulčić³

et al. 2016

Croat. Chem. Acta

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

Evic,

Soic,

Mocibob

et al. 2023

FEBS Letters

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We have previously identified a unique disulfide bond in the crystal structure of Arabidopsis cytosolic seryl‐tRNA synthetase involving cysteines evolutionarily conserved in all green plants. Here, we discovered that both cysteines are important for protein stability, but with opposite effects, and that their microenvironment may promote disulfide bond formation in oxidizing conditions. The crystal structure of the C244S mutant exhibited higher rigidity and an extensive network of noncovalent interactions correlating with its higher thermal stability. The activity of the wild‐type showed resistance to oxidation with H2O2, while the activities of cysteine‐to‐serine mutants were impaired, indicating that the disulfide link may enable the protein to function under oxidative stress conditions which can be beneficial for an efficient plant stress response.

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Synthetic and Editing Mechanisms of Aminoacyl-tRNA Synthetases

Perona

Gruić-Sovulj

2013

Topics in Current Chemistry

113

199

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Aminoacyl-tRNA synthetases (aaRS) ensure the faithful transmission of genetic information in all living cells. The 24 known aaRS families are divided into 2 structurally distinct classes (class I and class II), each featuring a catalytic domain with a common fold that binds ATP, amino acid, and the 3'-terminus of tRNA. In a common two-step reaction, each aaRS first uses the energy stored in ATP to synthesize an activated aminoacyl adenylate intermediate. In the second step, either the 2'- or 3'-hydroxyl oxygen atom of the 3'-A76 tRNA nucleotide functions as a nucleophile in synthesis of aminoacyl-tRNA. Ten of the 24 aaRS families are unable to distinguish cognate from noncognate amino acids in the synthetic reactions alone. These enzymes possess additional editing activities for hydrolysis of misactivated amino acids and misacylated tRNAs, with clearance of the latter species accomplished in spatially separate post-transfer editing domains. A distinct class of trans-acting proteins that are homologous to class II editing domains also perform hydrolytic editing of some misacylated tRNAs. Here we review essential themes in catalysis with a view toward integrating the kinetic, stereochemical, and structural mechanisms of the enzymes. Although the aaRS have now been the subject of investigation for many decades, it will be seen that a significant number of questions regarding fundamental catalytic functioning still remain unresolved.

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Substrate recognition and fidelity of maize seryl-tRNA synthetases

Cited by 12 publications

References 71 publications

Seryl-tRNA Synthetases in Translation and Beyond

Seryl-tRNA Synthetases in Translation and Beyond

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

Synthetic and Editing Mechanisms of Aminoacyl-tRNA Synthetases

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