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master's thesis
Karakterizacija Ankle1, nove ljudske endonukleaze koja sadrži LEM-domenu
Zagreb: University of Zagreb, Faculty of Science, 2011. urn:nbn:hr:217:625497
Zlopaša, Livija
University of Zagreb
Faculty of Science
Department of Biology

Institutional repository: Repository of the Faculty of Science

Cite this document

Zlopaša, L. (2011). Karakterizacija Ankle1, nove ljudske endonukleaze koja sadrži LEM-domenu (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:625497

Zlopaša, Livija. "Karakterizacija Ankle1, nove ljudske endonukleaze koja sadrži LEM-domenu." Master's thesis, University of Zagreb, Faculty of Science, 2011. https://urn.nsk.hr/urn:nbn:hr:217:625497

Zlopaša, Livija. "Karakterizacija Ankle1, nove ljudske endonukleaze koja sadrži LEM-domenu." Master's thesis, University of Zagreb, Faculty of Science, 2011. https://urn.nsk.hr/urn:nbn:hr:217:625497

Zlopaša, L. (2011). 'Karakterizacija Ankle1, nove ljudske endonukleaze koja sadrži LEM-domenu', Master's thesis, University of Zagreb, Faculty of Science, accessed 22 November 2024, https://urn.nsk.hr/urn:nbn:hr:217:625497

Zlopaša L. Karakterizacija Ankle1, nove ljudske endonukleaze koja sadrži LEM-domenu [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2011 [cited 2024 November 22] Available at: https://urn.nsk.hr/urn:nbn:hr:217:625497

L. Zlopaša, "Karakterizacija Ankle1, nove ljudske endonukleaze koja sadrži LEM-domenu", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2011. Available at: https://urn.nsk.hr/urn:nbn:hr:217:625497

Metadata
TitleKarakterizacija Ankle1, nove ljudske endonukleaze koja sadrži LEM-domenu
Title (english)Characterization of Ankle1 , a novel human LEM-domain containing endonuclease
AuthorLivija Zlopaša
MentorZdravko Lorković (mentor)
Committee memberZdravko Lorković (predsjednik povjerenstva)
Committee memberŽeljka Vidaković-Cifrek (član povjerenstva)
Committee memberGordana Lacković-Venturin (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Biology)
Zagreb
Defense date and country2011-09-22, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Biology
Abstract
LEM-proteini čine skupinu jezgrinih proteina sa zajedničkim strukturnim motivom dugim oko 40 aminokiselina nazvanim LEM-domena (ime je izvedeno iz imena proteina unutarnje jezgrine membrane: LAP2, emerin i MAN1). LEM-domena svih dosad analiziranih proteina posreduje u direktnom vezanju za BAF (barrier-to-autointegration factor). BAF je evolucijski visoko očuvani protein koji veže dvolančanu DNA, proteine jezgrine lamine, histone, te različite transkripcijske faktore. LEMproteini i BAF su otkriveni u višestaničnim organizmima, a nisu prisutni u jednostaničnim organizmima i biljkama. Ankle1 je novi i neobični protein koji sadrži LEM-domenu te, za razliku od većine ostalih LEMproteina, nije dio jezgrine membrane već se nalazi u nukleoplazmi. Predviđanje organizacije domena pokazuje da je Ankle1 očuvan tijekom evolucije od Caenorhabditis elegans do Homo sapiens. Ankle1 sadrži ankirinska ponavljanja, za koje se vjeruje da posreduju prilikom stvaranja interakcija među proteinima, LEM-domenu i GIY-YIG domenu, koja je opisana kao domena sa nukleaznom aktivnošću u skupini proteina nazvanih GIY-YIG endonukleaze. Predviđanja in silico otkrila su nukleotidne sljedove koji posreduju transport u i iz jezgre, koji se nalaze na očuvanim pozicijama unutar Ankle1 proteina, te koji nagoviještaju da se Ankle1 premješta između jezgre i citoplazme. Analiza uzorka ekspresije pokazala je da se Ankle1 izražava primarno u hematopoetskim tkivima, nagovještavajući moguću funkciju Ankle1 proteina tijekom razvoja i diferencijacije hematopoetskih staničnih linija.
Abstract (english)
LEM domain proteins are a group of nuclear proteins that share a common structural motif of approximately 40 amino acids, known as LEM domain (the name is derived from inner nuclear membrane proteins LAP2, emerin and MAN1). The LEM domain of all analysed proteins mediates association through direct binding to barrier-to-autointegration factor (BAF). BAF is a highly conserved protein that binds to dsDNA, nuclear lamina proteins, histones and various transcription factors. LEM domain proteins and BAF have been identified in multicellular organisms but are absent in unicellular eukaryotes and plants. Ankle1 is a novel unusual LEM domain protein which is, unlike most of the other LEM domain proteins, not an integral membrane protein, but localizes to the nucleoplasm. Prediction of its domain organization shows that Ankle1 is conserved throughout evolution from Caenorhabditis elegans to Homo sapiens. It contains ankyrin repeats, a LEM domain and a GIY-YIG domain, which has previously been described as a nuclease domain in a protein family called GIY-YIG endonucleases. In silico predictions revealed nuclear export sequences (NES) and nuclear localization sequences (NLS) at conserved positions within the Ankle1 protein, indicating that the protein shuttles between nucleus and cytoplasm. Expression pattern analysis showed that Ankle1 is expressed primarily in haematopoietic tissues and cell lines derived thereof, indicating a potential function during the development and differentiation of haematopoietic cells lineages.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:625497
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 conditionsAccess restricted to students and staff of home institution
Terms of useLicence In copyright icon
Created on2017-05-03 11:58:54