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

EVIC, Valentina, Ruzica SOIC, Marko MOCIBOB, Mario KEKEZ, Josef HOUSER, Michaela WIMMEROVÁ, Dubravka MATKOVIĆ-ČALOGOVIĆ, Ita GRUIC-SOVULJ, Ivana KEKEZ and Jasmina ROKOV-PLAVEC. Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation. FEBS Letters. Amsterdam: Elsevier Science, 2023, vol. 597, No 23, p. 2975-2992. ISSN 0014-5793. Available from: https://dx.doi.org/10.1002/1873-3468.14748.

Basic information

• Original name: Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation
• Authors: EVIC, Valentina, Ruzica SOIC, Marko MOCIBOB, Mario KEKEZ, Josef HOUSER (203 Czech Republic, belonging to the institution), Michaela WIMMEROVÁ (203 Czech Republic, belonging to the institution), Dubravka MATKOVIĆ-ČALOGOVIĆ, Ita GRUIC-SOVULJ, Ivana KEKEZ and Jasmina ROKOV-PLAVEC (guarantor).
• Edition: FEBS Letters, Amsterdam, Elsevier Science, 2023, 0014-5793.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10608 Biochemistry and molecular biology
• Country of publisher: Netherlands
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Impact factor: Impact factor: 3.500 in 2022
• RIV identification code: RIV/00216224:14740/23:00133310
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1002/1873-3468.14748
• UT WoS: 001083471700001
• Keywords in English: aminoacyl-tRNA synthetase; cysteine reactivity; disulfide bond; hydrogen peroxide; oxidative stress; thermal stability
• Tags: CF BIC, rivok
• Tags: International impact, Reviewed

Abstract

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.

Links

• EF18_046/0015974, research and development project: Name: Modernizace České infrastruktury pro integrativní strukturní biologii
• LM2023042, research and development project: Name: Česká infrastruktura pro integrativní strukturní biologii

Investor: Ministry of Education, Youth and Sports of the CR, CIISB - Czech Infrastructure for Integrative Structural Biology

• 90242, large research infrastructures: Name: CIISB III