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.

Základní údaje

Originální název

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

Autoři

EVIC, Valentina, Ruzica SOIC, Marko MOCIBOB, Mario KEKEZ, Josef HOUSER (203 Česká republika, domácí), Michaela WIMMEROVÁ (203 Česká republika, domácí), Dubravka MATKOVIĆ-ČALOGOVIĆ, Ita GRUIC-SOVULJ, Ivana KEKEZ a Jasmina ROKOV-PLAVEC (garant)

Vydání

FEBS Letters, Amsterdam, Elsevier Science, 2023, 0014-5793

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.500 v roce 2022

Kód RIV

RIV/00216224:14740/23:00133310

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1002/1873-3468.14748

UT WoS

001083471700001

Klíčová slova anglicky

aminoacyl-tRNA synthetase; cysteine reactivity; disulfide bond; hydrogen peroxide; oxidative stress; thermal stability

Štítky

CF BIC, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 27. 10. 2024 15:26, Ing. Martina Blahová

Anotace

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.

Návaznosti

EF18_046/0015974, projekt VaV

Název: Modernizace České infrastruktury pro integrativní strukturní biologii

90242, velká výzkumná infrastruktura

Název: CIISB III

Citovat

EVIC, Valentina, Ruzica SOIC, Marko MOCIBOB, Mario KEKEZ, Josef HOUSER, Michaela WIMMEROVÁ, Dubravka MATKOVIĆ-ČALOGOVIĆ, Ita GRUIC-SOVULJ, Ivana KEKEZ a 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, roč. 597, č. 23, s. 2975-2992. ISSN 0014-5793. Dostupné z: 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 a 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, roč.~597, č.~23, s.~2975-2992. ISSN~0014-5793. Dostupné z: https://dx.doi.org/10.1002/1873-3468.14748.

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