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- W17741392 abstract "The main subject of this thesis is the Sulphate Permease (SulP) protein family that includes more than two hundred members, identified in archaea, bacteria, fungi, plants and animals. Many of these proteins have been functionally characterized: most are anion exchangers or transporters with different substrate specificities and distinct mechanism of action (Saier et al., 1999). In mammals, the SulP family, known as Solute Linked Carrier 26 (SLC26), is composed of eleven members with important roles in normal physiology (Mount and Romero, 2004).The SulP proteins show a similar structural organization: a hydrophobic central core, which includes ten or twelve membrane helixes, and a less conserved C-terminal cytoplasmic portion that includes a STAS domain (Sulphate Transporter and Anti-Sigma factor antagonist domain). Despite the functional role of the STAS domain is still unclear, it appears to be crucial for the regulation of the transport activity (Ko et al., 2004; Zheng et al., 2005; Shibagaki and Grossman, 2006). Its fundamental role is also underlined by the fact that mutations that alter this domain in the SLC26 family can cause loss of function, resulting in serious genetic diseases, like diastrophic dysplasia or Pendred syndrome (Dawson and Markovich, 2005). No three-dimensional structure of STAS domains or full-length sequences is available for any SulP anion transporter. One part of the work was focused on the production of different forms of the STAS domain from different species, for the biophysical and structural characterization. Another part of the SulP project was performed at the Johann Wolfgang Goethe University of Frankfurt (Germany) and aimed at the production of some full-length SulP proteins, by a cell-free expression system, an emerging technique for the large-scale production of membrane proteins. In the last year, I was also involved in the crystallographic study of the Green Fluorescence Protein mutant, GFPmut2, in collaboration with Prof. Stefano Bettati of the University of Parma (Italy). The main aim of this work was the elucidation of the structural basis of the spectroscopic properties of this mutant, in particular with respect to changes in pH. The GFP chromophore can, in fact, exist either in a protonated or deprotonated state, with distinct spectral properties (Tsien, 1998). In a previous spectroscopic characterization, GFPmut2 (Ser65Ala, Val68Leu, Ser72Ala) was found more sensitive than the wild type GFP to pH changes in the physiological range (Chirico et al., 2002). The structures of GFPmut2 at pH 6 and pH 9 were determined at around 1.6 A resolution, allowing the correlation between the spectral and structural properties." @default.
- W17741392 created "2016-06-24" @default.
- W17741392 creator A5078011667 @default.
- W17741392 date "2009-02-02" @default.
- W17741392 modified "2023-09-27" @default.
- W17741392 title "Production and characterization of SulP anion transporters" @default.
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