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Identifier 000399323
Title Λειτουργική ανάλυση της πρωτεΐνης VIRP1
Alternative Title Functional analysis of the protein VIRP1
Author Μιχαλοπούλου, Βασιλική Α.
Thesis advisor Καλαντίδης, Κρίτωνας
Reviewer Τσαγρή, Ευθυμία
Κοτζαμπάσης, Κυριάκος
Abstract Bromodomains are present in diverse nuclear proteins, functioning as recruiting intermediates for transcriptional regulators and chromatin-modifying enzymes. Dysfunction of a bromodomaincontaining protein has been associated with the development of cancer. Recently, the BET (bromo and extraterminal) proteins, such as Brd4, have gained much attention after the development of potent bromodomain inhibitors. The bromodomain is a conserved region of 110 amino acids that forms 4 α- helices and 2 loops (ZA and BC), the latter capable of binding acetyl-lysine residues in histones and other proteins. In an effort identifying the essential hosts’ factors for PSTVd (Potato Spindle Tuber Viroid) interaction, Virp1 has been identified. It is the first plant bromodomain protein reported to bind RNA and has an essential role in PSTVd infectivity, as in Virp1-supressed plants PSTVd replication cannot be established. Nevertheless, the role of Virp1 has not yet been elucidated and so the objective of this master thesis is to understand its physiological role in plants, as well as its role in relation to the viroid. For this reason, we conducted point mutations in conserved amino acids of the domain, capable of influencing the cavity responsible for the activity of the domain either by closing (N269Y, V275F) or by enlarging it (N269A). There have been produced an artificial miRNA (amiRNA) in order to target endogenous Virp1 of the plant model Nicotiana benthamiana, as also bromo-domain mutated BY-2 (Nicotiana tabacum) cell lines were established. When investigating the sub-nuclear localization of the protein, it was found that VIRP1 localizes in nuclear speckles, areas rich in splicing factors, while only the wild-type protein has been detected in the centromeres during mitosis. Further, although the bromodomain of VIRP1 presents the same features to those of mammals ones, it was observed that it does not bind to any known inhibitor.
Language Greek
Subject Dromo-domain
Issue date 2016-03-18
Collection   School/Department--School of Sciences and Engineering--Department of Biology--Post-graduate theses
  Type of Work--Post-graduate theses
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