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Quarantini, S. (2012) Structural and functional study of Helicobacter pylori proteins contributing to stomach colonization. [Tesi di dottorato]

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Abstract (inglese)

Three H. pylori proteins contributing to stomach colonization have been chosen to be structurally characterized: Fur, Hp1454, and HypB.
The first one, which is a Fe-dependent transcription regulator was expressed and purified. Unfortunately. after the crystallization test started, the crystal structure of Fur was published by another group.
Hp1454 is a secreted protein of unknown function. It has been purified, expressed and crystallized. Since it lacks any sequence similarity with other proteins of known structure, Se-Met derivatives were produced and the structure determined. A function for the protein has been also proposed, based on the study of Hp1454 interaction network. The GTPase HypB is an essential factor for maturation of H. pylori’s hydrogenase and urease. It was cloned, expressed and purified and preliminary crystallization tests performed.

Abstract (italiano)

Tre proteine di H. pylori che rivestono un importante ruolo nella colonizzazione dello stomaco sono state scelte per essere caratterizzate strutturalmente: Fur, Hp1454 e HypB. La prima, un regolatore trascrizionale ferro-dipendente, è stata espressa e purificata. Purtroppo, dopo i primi test di cristallizzazione, la struttura di Fur è stata pubblicata da un altro gruppo. Hp1454 è una proteina secreta la cui funzione è sconosciuta. Hp1454 é stata purificata, espressa e cristallizzata. Poichè la proteina non presenta omologia di sequenza con altre proteine di struttura nota, sono stati prodotti derivati di Se-Met e la struttura è stata quindi determinata. Una funzione per la proteina è stata inoltre proposta sulla base degli studi di interazione tra Hp1454 e altre proteine. La GTPasi HypB è un essenziale fattore nella maturazione dell' idrogenasi e dell' ureasi di pylori. La proteina è stata clonata e purificata e sono stati effettuate delle prove preliminari di cristallizzazione.

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Tipo di EPrint:Tesi di dottorato
Relatore:Zanotti, Giuseppe
Dottorato (corsi e scuole):Ciclo 24 > Scuole 24 > BIOSCIENZE E BIOTECNOLOGIE > BIOTECNOLOGIE
Data di deposito della tesi:25 Gennaio 2012
Anno di Pubblicazione:27 Gennaio 2012
Parole chiave (italiano / inglese):H. pylori, HP1454, lipoprotein, secretion, Tol-Pal system, SAD, HypB.
Settori scientifico-disciplinari MIUR:Area 05 - Scienze biologiche > BIO/10 Biochimica
Struttura di riferimento:Dipartimenti > pre 2012 Dipartimento di Chimica Biologica
Codice ID:4478
Depositato il:17 Dic 2012 10:57
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21. Spudich J.Spotlight on receptor/transducer interaction.Nat Struct Biol. 2002 Nov;9(11):797-9. Cerca con Google

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23. Spudich JL.Variations on a molecular switch: transport and sensory signalling by archaeal rhodopsins.Mol Microbiol. 1998 Jun;28(6):1051-8. Cerca con Google

24. Vogeley L, Luecke H.Crystallization, X-ray diffraction analysis and SIRAS/molecular-replacenent phasing of three crystal forms of Anabaena sensory rhodopsin transducer.Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt 4):388-91. Cerca con Google

25. Vogeley L, Sineshchekov OA, Trivedi VD, Sasaki J, Spudich JL, Luecke H.Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 A.Science. 2004 Nov 19;306(5700):1390-3. Cerca con Google

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27. Wang S, Kim SY, Jung KH, Ladizhansky V, Brown LS. A eukaryotic-like interaction of soluble cyanobacterial sensory rhodopsin transducer with DNA. J Mol Biol. 2011 Aug 12;411(2):449-62. Cerca con Google

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