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master's thesis
Proteinske domene aminoacil-tRNAsintetaza i interakcije s drugim proteinima
Zagreb: University of Zagreb, Faculty of Science, 2009. urn:nbn:hr:217:521645
Podolski, Marija
University of Zagreb
Faculty of Science
Department of Biology

Institutional repository: Repository of the Faculty of Science

Cite this document

Podolski, M. (2009). Proteinske domene aminoacil-tRNAsintetaza i interakcije s drugim proteinima (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:521645

Podolski, Marija. "Proteinske domene aminoacil-tRNAsintetaza i interakcije s drugim proteinima." Master's thesis, University of Zagreb, Faculty of Science, 2009. https://urn.nsk.hr/urn:nbn:hr:217:521645

Podolski, Marija. "Proteinske domene aminoacil-tRNAsintetaza i interakcije s drugim proteinima." Master's thesis, University of Zagreb, Faculty of Science, 2009. https://urn.nsk.hr/urn:nbn:hr:217:521645

Podolski, M. (2009). 'Proteinske domene aminoacil-tRNAsintetaza i interakcije s drugim proteinima', Master's thesis, University of Zagreb, Faculty of Science, accessed 25 November 2024, https://urn.nsk.hr/urn:nbn:hr:217:521645

Podolski M. Proteinske domene aminoacil-tRNAsintetaza i interakcije s drugim proteinima [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2009 [cited 2024 November 25] Available at: https://urn.nsk.hr/urn:nbn:hr:217:521645

M. Podolski, "Proteinske domene aminoacil-tRNAsintetaza i interakcije s drugim proteinima", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2009. Available at: https://urn.nsk.hr/urn:nbn:hr:217:521645

Metadata
TitleProteinske domene aminoacil-tRNAsintetaza i interakcije s drugim proteinima
Title (english)Protein domains of aminoacyl-tRNA synthetases and interactions with other proteins
AuthorMarija Podolski
MentorIvana Weygand-Đurašević (mentor)
Committee memberIvana Weygand-Đurašević (predsjednik povjerenstva)
Committee memberMirjana Kalafatić (član povjerenstva)
Committee memberDijana Škorić (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Biology)
Zagreb
Defense date and country2009, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Biology
Abstract
Prethodno otkrivena kristalna struktura seril-tRNA-sintetaze (SerRS) metanogenog tipa iz arheje Methanosarcina barkeri ukazala je na neke atipične karakteristike ovog enzima, jedna od kojih je bila i prisutnost motiva HTH unutar C-terminalne domene proteina. Za njega se pretpostavljalo da je ima važnu ulogu pri dimerizaciji SerRS i interakciji između N- i Cterminalnih domena proteina. Ova pretpostavka je potvrđena našim rezultatima dobivenim metodom dvaju hibrida. Osim toga, pretraživanje metodom dvaju hibrida iskorišteno je za utvrđivanje proteina s kojima SerRS iz Methanothermobacter thremautotrophicus interagira, jedan od kojih je bila i arginiltRNA- sintetaza (ArgRS). Ovu interakciju smo potvrdili afinitetnom kromatografijom („GSTpulldown assay“). Prethodno je pronađeno da neke SerRS metanogenog tipa mogu, osim pripadnih tRNASer i tRNASec prepoznati i eukariotske i prokariotske tRNASer. Naši rezultati predlažu da je to slučaj i kod SerRS iz M. thermautotrophicus.
Abstract (english)
Recently resolved crystal structure of methanogenic type seryl-tRNA synthetase (SerRS) from Methanosarcina barkeri revealed some atypical features, one of which was an idiosyncratic helix-turn-helix motif within C-terminal domain of the protein. This motif seems to be important for dimerization of the enzyme and interaction between Nand C-terminal domains. This assumption was supported by our experimental results achieved by yeast two-hybrid assays. In addition, the yeast two-hybrid approach was used to screen for proteins interacting with SerRS in Methanothermobacter thermautotrophicus. One of the proteins which was found to interact with SerRS was arginyl-tRNA synthetase. To support this finding, we proved this interaction by affinity chromatography (GST-pulldown assay). As it was established for some methanogenic type SerRSs previously, some of these enzymes are capable of recognizing both eukaryotic and prokariotyc tRNASer in addition to the homologous tRNASer and tRNASec substrates. Our results indicate that this feature is also displayed by M.thermautotrophicus SerRS.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:521645
Study programmeTitle: Molecular Biology
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra molekularne biologije (magistar/magistra molekularne biologije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2018-03-15 09:43:19