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Nickel is a fundamental micronutrient for cellular life, but it is toxic in soluble form at nonphysiological concentrations. Such potentially contradictory features required living organisms to develop efficient systems for nickel utilization and homeostasis. This is the case for incorporation of nickel into the active site of urease, a multistep, tightly regulated process, requiring the interplay of various accessory proteins. The understanding of this activation mechanism may find medical applications against ureolytic bacteria, among which Mycobacterium tuberculosis is a deadly pathogen for humans. The topic of this study is UreG, an essential chaperone in the in vivo activation of urease upon insertion of Ni 2+ into the active site. The protein was examined using both experimental and computational approaches.

In particular, the soluble M. Tuberculosis UreG ( MtUreG) was overexpressed in Escherichia coli and purified to homogeneity. The identity of the isolated protein was established by mass spectrometry. On-line size-exclusion chromatography and light scattering indicated that MtUreG exists as a dimeric form in solution.

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Determination of the free thiol concentration revealed that a disulfide bond is present in the dimer. The isolated MtUreG shows low GTPase activity under native conditions, with a k cat of 0.01 min -1.

Circular dichroism spectroscopy demonstrated the presence of a well-defined secondary structure (8% α-helices, 29% β-strands) in MtUreG, whereas NMR spectroscopy indicated that this protein does not behave as a rigid three-dimensional fold and thus can be assigned to the class of intrinsically unstructured polypeptides. The molecular model of MtUreG in the fully folded and functional form was built using fold recognition algorithms. An extensive similarity search was performed to determine conservation patterns in all known bacterial UreG sequences. The generation of a multiple-sequence alignment and the related phylogenetic tree allowed us to recognize key residues and motifs that are likely important for protein function. A structural database containing the homology-built models of the most representative UreG proteins was created, confirming the structural analogies among the UreG family. A flexible region, likely to be important for protein function, is identified.

The structural conservation among this class of GTPases is discussed on the basis of their function in the urease assembly process. • Ca' Foscari University of Venice • Cagliari State University • Free University of Bolzano • Politecnico di Bari • Scuola Superiore Sant'Anna • University of Bologna • University of Camerino • University of Genoa • University of Messina • University of Naples Federico II • University of Padova • University of Palermo • University of Parma • University of Pavia • University of Perugia • University of Pisa • University of Roma TRE • University of Rome Tor Vergata • University of Salerno • University of Siena • University of Verona.