prikaz prve stranice dokumenta Uloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres
Embargo period 2026-03-07
doctoral thesis
Uloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres
Zagreb: University of Zagreb, Faculty of Science, 2024. urn:nbn:hr:217:345036
Ević, Valentina
University of Zagreb
Faculty of Science
Department of Chemistry

Institutional repository: Repository of the Faculty of Science

Cite this document

Ević, V. (2024). Uloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres (Doctoral thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:345036

Ević, Valentina. "Uloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres." Doctoral thesis, University of Zagreb, Faculty of Science, 2024. https://urn.nsk.hr/urn:nbn:hr:217:345036

Ević, Valentina. "Uloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres." Doctoral thesis, University of Zagreb, Faculty of Science, 2024. https://urn.nsk.hr/urn:nbn:hr:217:345036

Ević, V. (2024). 'Uloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres', Doctoral thesis, University of Zagreb, Faculty of Science, accessed 17 May 2024, https://urn.nsk.hr/urn:nbn:hr:217:345036

Ević V. Uloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres [Doctoral thesis]. Zagreb: University of Zagreb, Faculty of Science; 2024 [cited 2024 May 17] Available at: https://urn.nsk.hr/urn:nbn:hr:217:345036

V. Ević, "Uloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres", Doctoral thesis, University of Zagreb, Faculty of Science, Zagreb, 2024. Available at: https://urn.nsk.hr/urn:nbn:hr:217:345036

Metadata
TitleUloga aminoacil-tRNA-sintetaza u staničnom odgovoru na oksidacijski stres
Title (english)The role of aminoacyl-tRNA synthetases in cellular oxidative stress response
AuthorValentina Ević
MentorJasmina Rokov Plavec (mentor)
Committee memberIvana Ivančić Baće (predsjednik povjerenstva)
Committee memberIvana Leščić Ašler (član povjerenstva)
Committee memberMorana Dulić (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Chemistry)
Zagreb
Defense date and country2024-03-07, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Universal decimal classification
(UDC)		54 - Chemistry. Crystallography. Mineralogy
Abstract
Aminoacil-tRNA-sintetaze (AARS) su enzimi koji kataliziraju nastanak kovalentne veze između pripadne aminokiseline i tRNA pri čemu nastaje aminoacil-tRNA, supstrat u procesu translacije. Citosolne AARS zbog redukcijskog okoliša inače nemaju disulfidnu vezu, no pronađena je u kristalnoj strukturi citosolne seril-tRNA-sintetaze (SerRS) iz biljke Arabidopsis thaliana. U ovom radu dizajnirane su jednostruko (SerRS_C213S, SerRS_C244S) i dvostruko mutirane inačice (SerRS_C213S/C244S) i pokazano je da dolazi do reverzibilnog nastajanja disulfidne veze što omogućuje enzimu nepromijenjenu aktivnost u oksidacijskom stresu. Također je istražen utjecaj mistranslacije uzrokovane ugradnjom valina (Val) ili norvalina (Nva) umjesto izoleucina na odgovor na oksidacijski stres. U tu svrhu korišteni su sojevi bakterije Escherichia coli koji eksprimiraju izoleucil-tRNA-sintetazu s inaktiviranom domenom za popravak pogreške (PS7066 i ED-). Rezultati su pokazali da prethodni uzgoj stanica u mistranslatirajućim uvjetima do stacionarne faze uzrokuje bolje preživljenje i rast u oksidacijskom stresu u odnosu na stanice koje nisu rasle u mistranslatirajućim uvjetima. Nadalje, uočeno je da uzgoj stanica s inaktiviranim RpoS-om u mediju s višim koncentracijama valina ili norvalina izaziva adaptaciju na oksidacijski stres koja je neovisna o RpoS-u, dok stanice uzgojene pri nižim koncentracijama valina ili norvalina ne preživljavaju u uvjetima oksidacijskog stresa.
Abstract (english)
Aminoacyl-tRNA synthetases (AARS) are enzymes that catalyze covalent bond formation between cognate amino acid and tRNA to produce aminoacyl-tRNA - substrate in the translation process. Due to the reductive environment, cytosolic AARSs do not have disulfide bonds, however, one was found in the crystal structure of cytosolic seryl-tRNA synthetase (SerRS) from the plant Arabidopsis thaliana. In this study, point (SerRS_C213S, SerRS_C244S) and double mutants (SerRS_C213S/C244S) were designed and it was shown that the reversible disulfide bond formation allows unchanged enzyme activity under oxidative stress. Also, the effect of isoleucine-to-valine (Val) or norvaline (Nva) mistranslation on oxidative stress response was investigated. For this purpose, Escherichia coli strains expressing isoleucyl-tRNA synthetase with a mutation in the editing domain were used (PS7066 and ED-). The results show that prior cell growth in mistranslating conditions to stationary phase leads to higher survival and growth rates under oxidative stress compared to cells that were not grown in mistranslating conditions. Furthermore, it was shown that prior growth of cells with inactivated RpoS in media with higher concentrations of Val or Nva leads to adaptation to oxidative stress that is RpoS- independent, while the cells grown with lower concentrations of Val or Nva do not survive in oxidative stress conditions.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:345036
Promotion2024
Study programmeTitle: Doctoral study
Study programme type: university
Study level: postgraduate
Academic / professional title: doktor/doktorica u području prirodnih znanosti (doktor/doktorica u području prirodnih znanosti)
Type of resourceText
Extent130, XXXIII str. ; 30 cm
File originBorn digital
Access conditionsEmbargoed access
Embargo expiration date: 2026-03-07
Terms of useLicence In copyright icon
Created on2024-03-11 12:23:39