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undergraduate thesis
Ubikvitin i bolesti povezane s nepravilnom ubikvitinacijom
2019. urn:nbn:hr:166:904536
Vukasović-Lončar, Vedrana
University of Split
Faculty of Science
Department of Chemistry

Cite this document

Vukasović Lončar, V. (2019). Ubikvitin i bolesti povezane s nepravilnom ubikvitinacijom (Undergraduate thesis). Split: University of Split, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:166:904536

Vukasović Lončar, Vedrana. "Ubikvitin i bolesti povezane s nepravilnom ubikvitinacijom." Undergraduate thesis, University of Split, Faculty of Science, 2019. https://urn.nsk.hr/urn:nbn:hr:166:904536

Vukasović Lončar, Vedrana. "Ubikvitin i bolesti povezane s nepravilnom ubikvitinacijom." Undergraduate thesis, University of Split, Faculty of Science, 2019. https://urn.nsk.hr/urn:nbn:hr:166:904536

Vukasović Lončar, V. (2019). 'Ubikvitin i bolesti povezane s nepravilnom ubikvitinacijom', Undergraduate thesis, University of Split, Faculty of Science, accessed 17 November 2024, https://urn.nsk.hr/urn:nbn:hr:166:904536

Vukasović Lončar V. Ubikvitin i bolesti povezane s nepravilnom ubikvitinacijom [Undergraduate thesis]. Split: University of Split, Faculty of Science; 2019 [cited 2024 November 17] Available at: https://urn.nsk.hr/urn:nbn:hr:166:904536

V. Vukasović Lončar, "Ubikvitin i bolesti povezane s nepravilnom ubikvitinacijom", Undergraduate thesis, University of Split, Faculty of Science, Split, 2019. Available at: https://urn.nsk.hr/urn:nbn:hr:166:904536

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Metadata
TitleUbikvitin i bolesti povezane s nepravilnom ubikvitinacijom
Title (english)Ubiquitin and diseases associated with irregular ubiquitination
AuthorVedrana Vukasović-Lončar
MentorMaja Pavela Vrančić (mentor)
Committee memberMaja Pavela Vrančić (predsjednik povjerenstva)
Committee memberIvica Ljubenkov (član povjerenstva)
Committee memberStjepan Orhanović (član povjerenstva)
GranterUniversity of Split
Faculty of Science
(Department of Chemistry)
Split
Defense date and country2019-09-11, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
Proteini su biološki važne funkcionalne molekule koje obavljaju brojne zadaće prema uputama gena. Da bi bili funkcionalni, moraju biti pravilno uvijeni u trodimenzionalnu strukturu. Ako na tom putu dođe do pogrešaka, proteine obilježava mali protein ubikvitin. Ubikvitinaciju kataliziraju ubikvitin-aktivirajući enzim (E1), ubikvitin-konjugirajući enzim (E2) i ubikvitin-protein-ligaza (E3). Prvo se ubikvitin aktivira hidrolizom ATP-a te se C- terminalnim krajem veže na sulfhidrilnu skupinu E1 enzima stvarajući tioestersku vezu. Zatim E2 enzim prenosi aktivirani ubikvitin na svoju sulfhidrilnu skupinu stvarajući tako novu tioestersku vezu. Završni korak je prijenos ubikvitina s E2 na supstrat što katalizira E3 ligaza. Ubikvitin se C-terminalnim krajem veže za neki od lizinskih ostataka supstrata uz nastanak čvrste izopeptidne veze. Ovisno o načinu i broju vezanih molekula ubikvitina, protein se može usmjeriti u različite stanične procese. Najčešća je razgradnja u proteasomu gdje se proteini razmotaju i cijepaju na kraće peptidne fragmente. Pogreškama u ubikvitinaciji može doći do mnogih neurodegenerativnih bolesti i tumora.
Abstract (english)
Proteins are biologically important functional molecules that carry out numerous tasks according to gene guidelines. To be functional, they must be properly folded into a threedimensional structure. If mistakes occur on this pathway, proteins are labelled by a small protein, ubiquitin. Ubiquitination is catalyzed by an ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin-protein-ligase (E3). First, ubiquitin is activated on account of ATP hydrolysis, and with its C-terminus binds to the sulfhydryl group of the E1 enzyme generating a thioester bond. Then, the E2 enzyme transfers the activated ubiquitin to its sulfhydryl group creating a new thioester bond. The final step is the transfer of ubiquitin from E2 to a protein substrate, catalyzed by the E3 ligase. Ubiquitin, with its Cterminal end, binds to a specific lysine residue of the substrate and a tight isopeptide bond is formed. Depending on the way and number of bonded ubiquitin molecules, the protein can be directed into different cellular processes. The most common is the proteasomal degradation where proteins are cleaved and reduced to shorter peptide fragments. Disregulation of ubiquitination can result in many neurodegenerative diseases and tumors.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:166:904536
Study programmeTitle: Nutrition
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) nutricionizma (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) nutricionizma)
Type of resourceText
File originBorn digital
Access conditionsAccess restricted to students and staff of home institution
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Created on2019-11-22 12:14:46