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master's thesis
Oligomerizacijsko stanje transkripcijskog regulatora QacR iz bakterije Staphylococcus aureus
Split: University of Split, Faculty of Science, 2023. urn:nbn:hr:166:275413
Vitovski, Mihaela
University of Split
Faculty of Science
Department of Chemistry

Institutional repository: Repository of Faculty of Science

Cite this document

Vitovski, M. (2023). Oligomerizacijsko stanje transkripcijskog regulatora QacR iz bakterije Staphylococcus aureus (Master's thesis). Split: University of Split, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:166:275413

Vitovski, Mihaela. "Oligomerizacijsko stanje transkripcijskog regulatora QacR iz bakterije Staphylococcus aureus." Master's thesis, University of Split, Faculty of Science, 2023. https://urn.nsk.hr/urn:nbn:hr:166:275413

Vitovski, Mihaela. "Oligomerizacijsko stanje transkripcijskog regulatora QacR iz bakterije Staphylococcus aureus." Master's thesis, University of Split, Faculty of Science, 2023. https://urn.nsk.hr/urn:nbn:hr:166:275413

Vitovski, M. (2023). 'Oligomerizacijsko stanje transkripcijskog regulatora QacR iz bakterije Staphylococcus aureus', Master's thesis, University of Split, Faculty of Science, accessed 30 May 2024, https://urn.nsk.hr/urn:nbn:hr:166:275413

Vitovski M. Oligomerizacijsko stanje transkripcijskog regulatora QacR iz bakterije Staphylococcus aureus [Master's thesis]. Split: University of Split, Faculty of Science; 2023 [cited 2024 May 30] Available at: https://urn.nsk.hr/urn:nbn:hr:166:275413

M. Vitovski, "Oligomerizacijsko stanje transkripcijskog regulatora QacR iz bakterije Staphylococcus aureus", Master's thesis, University of Split, Faculty of Science, Split, 2023. Available at: https://urn.nsk.hr/urn:nbn:hr:166:275413

Metadata
TitleOligomerizacijsko stanje transkripcijskog regulatora QacR iz bakterije Staphylococcus aureus
Title (english)Oligomerization state of the transcriptional regulator QacR from the bacterium Staphylococcus aureus
AuthorMihaela Vitovski
MentorMatilda Šprung (mentor)
MentorDoris Crnčević (pomoć pri izradi, neposredni voditelj)
Committee memberMatilda Šprung (predsjednik povjerenstva)
Committee memberStjepan Orhanović (član povjerenstva)
Committee memberDoris Crnčević (član povjerenstva)
GranterUniversity of Split
Faculty of Science
(Department of Chemistry)
Split
Defense date and country2023-07-18, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
QacR je protein patogenih bakterija Staphylococcus aureus koji regulira razinu transkripcije qacA gena. Ovaj gen je odgovoran za ekspresiju efluks pumpe QacA koja je povezana s rezistencijom bakterije S. aureus na antibiotike. Pravilna oligomerizacija regulatornog proteina QacR utječe na njegov afinitet prema DNA i na regulaciju ekspresije efluks pumpe QacA. Danas se sve češće za analizu oligomerizacije proteina primjenjuju nativne tehnike elektroforeze. U ovome radu za provjeru oligomerizacijskog stanja transkripcijskog regulatora QacR korištena je BN-PAGE elektroforeza. BN-PAGE elektroforezom je pokazano da QacR spontano dimerizira nakon inkubacije na sobnoj temperaturi što je potvrdio i imunoblot s anti-His protutijelom. Budući da su eksperimenti provedeni s dMUT QacR varijantom proteina koja nosi zamjene na položajima \(Cys^{72}\) i \(Cys^{141}\), možemo zaključiti da spontana dimerizacija nije uvjetovana stvaranjem disulfidnih veza već vjerojatno velikom dodirnom površinom koju dijele dva monomera.
Abstract (english)
QacR is a protein of the pathogenic bacterium Staphylococcus aureus that regulates the transcription of the qacA gene. This gene is responsible for the expression of the efflux pump QacA, which is associated with antibiotic resistance in S. aureus. Proper oligomerization of the regulatory protein QacR affects its affinity for DNA and regulation of efflux pump QacA expression. Nowadays, native electrophoresis techniques are increasingly used to analyze protein oligomerization. In this work, BN-PAGE electrophoresis was used to check the oligomerization state of the transcriptional regulator QacR. BN-PAGE electrophoresis showed that QacR dimerized spontaneously after incubation at room temperature, which was also confirmed by immunoblot with anti-His antibody. Since the experiments were performed with the dMUT-QacR protein variant carrying substitutions at positions \(Cys^{72}\) and \(Cys^{141}\), we can conclude that the spontaneous dimerization is not due to disulfide bond formation but to the large contact area between the two monomers.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:166:275413
Study programmeTitle: Biology and Chemistry; specializations in: major in teaching
Course: major in teaching
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra edukacije biologije i kemije (magistar/magistra edukacije biologije i kemije)
Type of resourceText
File originBorn digital
Access conditionsAccess restricted to authenticated users
Terms of useLicence In copyright icon
Created on2023-07-19 12:58:28