ΠΜΣ Μικροβιακή ΒιοτεχνολογίαLibrary of the School of Science
Κων/νος Βοργιάς Καθηγητής (Επιβλέπων), Γεώργιος Διαλλινάς Καθηγητής, Δημήτριος Χατζηνικολάου Επίκ. Καθηγητής
Λειτουργική ανάλυση της HUTth πρωτεΐνης από το θερμόφιλο βακτήριο Thermus thermophilus και in silico ανάλυση ομόλογων HU πρωτεϊνών
Functional studies of the HUTth protein from Thermus thermophilus and in silico analyses of HU homologs
In prokaryotes, the chromosomal DNA is organized into a non-typical
defined structure called nucleoid in which a considerable number of proteins,
the histone-like DNA-binding proteins, play a major role in the compaction of
bacterial chromatin. The most abundant and the best characterized
members of this group are the HU (Heat-Unstable nucleoid protein). The
histone-like DNA-binding proteins (HU) are a convenient model for
studying factors affecting thermostability because of their relatively simple,
easily comparable structures, their common function, and their presence
in organisms of widely differing thermostability.
In this thesis, we studied the HUTth protein from Thermus thermophilus by
conducting biochemical, biophysical and structural analyses experiments.
Besides, through extensive bioinformatics and phylogenetic analysis, we
identified the factors that affect the thermostability of the HU protein and we
analyzed the strategies chosen by the thermophilic bacteria to deal with the
thermal stability in this protein family.
Protein thermostability, Bacterial histone-like proteins, Ancestral Sequence Reconstruction, Thermus thermophilus, hu
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