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

J 2023

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 et. al.

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

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

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

Abstract

V originále

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

90242, large research infrastructures

Name: CIISB III

Citovat

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.

@article{2367499,
   author = {Evic, Valentina and Soic, Ruzica and Mocibob, Marko and Kekez, Mario and Houser, Josef and Wimmerová, Michaela and MatkovićandČalogović, Dubravka and GruicandSovulj, Ita and Kekez, Ivana and RokovandPlavec, Jasmina},
   article_location = {Amsterdam},
   article_number = {23},
   doi = {http://dx.doi.org/10.1002/1873-3468.14748},
   keywords = {aminoacyl-tRNA synthetase; cysteine reactivity; disulfide bond; hydrogen peroxide; oxidative stress; thermal stability},
   language = {eng},
   issn = {0014-5793},
   journal = {FEBS Letters},
   title = {Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation},
   url = {https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14748},
   volume = {597},
   year = {2023}
}

TY  - JOUR
ID  - 2367499
AU  - Evic, Valentina - Soic, Ruzica - Mocibob, Marko - Kekez, Mario - Houser, Josef - Wimmerová, Michaela - Matković-Čalogović, Dubravka - Gruic-Sovulj, Ita - Kekez, Ivana - Rokov-Plavec, Jasmina
PY  - 2023
TI  - Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation
JF  - FEBS Letters
VL  - 597
IS  - 23
SP  - 2975-2992
EP  - 2975-2992
PB  - Elsevier Science
SN  - 00145793
KW  - aminoacyl-tRNA synthetase
KW  - cysteine reactivity
KW  - disulfide bond
KW  - hydrogen peroxide
KW  - oxidative stress
KW  - thermal stability
UR  - https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14748
N2  - 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.
ER  -

EVIC, Valentina, Ruzica SOIC, Marko MOCIBOB, Mario KEKEZ, Josef HOUSER, Michaela WIMMEROVÁ, Dubravka MATKOVI$\backslash$'C-ČALOGOVI$\backslash$'C, 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. \textit{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.

Detailed Information on Publication Record