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Identifier |
000399323 |
Title |
Λειτουργική ανάλυση της πρωτεΐνης VIRP1 |
Alternative Title |
Functional analysis of the protein VIRP1 |
Author
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Μιχαλοπούλου, Βασιλική Α.
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Thesis advisor
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Καλαντίδης, Κρίτωνας
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Reviewer
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Τσαγρή, Ευθυμία
Κοτζαμπάσης, Κυριάκος
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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.
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Language |
Greek |
Subject |
Dromo-domain |
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PSTVd |
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Viroid |
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Βρόμο-επικράτεια |
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Ιοειδές |
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Πρωτεΐνη |
Issue date |
2016-03-18 |
Collection
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School/Department--School of Sciences and Engineering--Department of Biology--Post-graduate theses
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Type of Work--Post-graduate theses
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Permanent Link |
https://elocus.lib.uoc.gr//dlib/9/2/6/metadata-dlib-1455093864-690260-10630.tkl
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Views |
354 |