Characterization of Ankle1, a novel human LEM-domain containing endonuclease

Zlopaša, Livija (2011) Characterization of Ankle1, a novel human LEM-domain containing endonuclease. Diploma thesis, Faculty of Science > Department of Biology.

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Abstract

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.

Item Type: Thesis (Diploma thesis)
Keywords: Ankle1, LEM proteins, NES, NLS. GIY-YIG nuclease domain
Supervisor: Lorković, Zdravko
Date: 2011
Number of Pages: 74
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Silvana Šehić
Date Deposited: 01 Sep 2014 12:42
Last Modified: 18 Sep 2014 11:22
URI: http://digre.pmf.unizg.hr/id/eprint/2575

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