Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae

master's thesis

• Title (english): Htm2-A specific enzyme from yeast Saccharomyces cerevisiae
• Author: Iva Patron
• Mentor: Vladimir Mrša (mentor)
• Granter: University of Zagreb; Faculty of Food Technology and Biotechnology; (Department of Chemistry and Biochemistry); (Laboratory for Biochemistry); Zagreb
• Defense date and country: 2014-09-23, Croatia
• Scientific / art field, discipline and subdiscipline: BIOTECHNICAL SCIENCES; Biotechnology

Abstract

U eukariotskim stanicama, membranski proteini i topljivi proteini sekretornog puta nakon sinteze ulaze u endoplazmatski retikulum (ER) u nesmotanom obliku. Direktno nakon ulaska u ER, većina proteina je glikolizirana odrađenim ugljikohidratima na određenom mjestu glikozilacije nakon čega proteini započinju smatanje. Protein koji se ne može pravilno smotati, bit će obilježen i degradiran u procesu nazvanom razgradnja proteina u endoplazmatskom retikulumu. Istraživanja su pokazala da se tijekom procesa N-glikozilacije proteina, značajna količina slobodnih oligosaharida sintetizira u ER-u. Slobodni oligosaharidi se također sintetiziraju u citosolu enzimskim procesom deglikozilacije krivo smotanih glikoproteina. Pogreške pri razgradnji proteina u ER-u, bilo gubitkom funkcije ili preranom degradacijom proteina, uzrokuju brojne teške bolesti. Upravo zbog toga, otkrivanje novih komponenata sustava za razgradnju proteina u ER-u kako bi ga bolje razumijeli, od izrazite je važnosti. U ovom radu, nova potencijalna kvaščeva manozidaza, Htm2 poznata i kao Mnl2, je identificirana i istraživana, a istraživanja su pokazala da se nalazi u Golgijevom aparatu.

Abstract (english)

In eukaryotes, membrane and soluble proteins of the secretory pathway enter the endoplasmic reticulum (ER) after synthesis in an unfolded state. Directly after entry, most proteins are modified with glycans at suitable glycosylation sites and start to fold. A protein that cannot fold properly will be degraded in a process called ER associated degradation (ERAD). It has been shown that during the N-glycosylation of proteins, significant amounts of free oligosaccharides are generated in the lumen of the ER. Free OSs are also formed in the cytosol by enzymatic deglycosylation of misfolded glycoproteins. Failures in ERAD, either by loss of function or by premature degradation of proteins, are a cause of severe disease. Therefore, the search for novel ERAD components to gain better insight in this process is of high importance. In this work a novel putative yeast mannosidase, named Htm2 also known as Mnl2, located in Golgi was explored and identified.

• Keywords: razgradnja proteina u ER-u; N-glikozilacija; slobodni oligosaharidi; manozidaza; sekretorni put
• Keywords (english): ERAD; N-glycosylation; free oligosaccharides; mannosidase; secretory pathway
• Language: croatian
• URN:NBN: urn:nbn:hr:159:999380
• Study programme: Title: Molecular Biotechnology; Study programme type: university; Study level: graduate; Academic / professional title: magistar/magistra inženjer/inženjerka molekularne biotehnologije (magistar/magistra inženjer/inženjerka molekularne biotehnologije)
• Type of resource: Text
• File origin: Born digital
• Access conditions: Access restricted to students and staff of home institution
• Created on: 2017-05-02 10:42:26