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Unravelling functional interactions of the rhodanese-like protein RhdA of azobacter vinelandii : dottorato di ricerca in biochimica : tesi di dottorato

Cartini, Francesca <1979- >

Tesi o dissertazioni - 2008

RhdA-SSH could function as “escort” protein during sulfur mobilization processes. E.coli IscS promote the RhdA persulfuration, that exhibits Michaelis-Menten behaviour. Both A. vinelandii cysteine desulfurases were able to generate RhdA-SSH but only NifS exhibits Michaelis-Menten behaviour. The NifS alanine activity resulted higher than that of IscS; in the presence of RhdA, the IscS activity was increased up to 58%. Formation of IscS-SSH was higher than that of NifS-SSH; in the presence of RhdA, the persulfuration of both cysteine desulfurases was increased. Size-exclusion and affinity chromatography were carried out to search possible metabolic interactions of RhdA-SSH. Unfortunately, we were not able to define whether a complex between RhdA and the cysteine desulfurases or some other interacting proteins could be formed. Using an A. vinelandii strain lacking rhdA gene and an E. coli strain lacking sseA gene, we characterized some response to induced oxidative stress. A vinelandii UW136 [...]
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