Scheda di dettaglio – i prodotti della ricerca
| Dato | Valore |
|---|---|
| Title | Identification of protein partners of the Azotobacter vinelandii rhodanese-like protein RhdA by pull-down approaches |
| Abstract | Rhodaneses (TST; EC 2.8.1.1) catalyze in vitro the transfer of sulfane sulfur from thiosulfate to cyanide with the concomitant formation of thiocyanate. Genome sequence analyses evidenced the presence of more than 14000 sequences coding for putative rhodanese-like proteins (RDPs). These sequences are distributed in all taxa thus suggesting RDPs involvement in biological processes different from cyanide detoxification. Studies aiming to unravel RDP biological functions highlighted the relationship between members of this superfamily and the maintenance of the intracellular redox homeostasis. This ability may rely in the peculiar RDP catalytic domain that consists of a cysteine residue centered in an electropositive environment that promotes the stabilization of the bio-active persulfide sulfur. The aim of this work was to gain more insights about RDP biological function by the identification of protein interaction partners. For this reason we used tagged recombinant versions of the biochemically characterized RDP RhdA from Azotobacter vinelandii, as a bait to isolate interaction partners by pull-down approaches. We identified IlvC, an oxidative sensitive ketol-acid reductoisomerase (KARI; EC 1.1.1.86). The partial inhibition of KARI activity in the A. vinelandii RhdA-null mutant strain suggests a functional interaction between RhdA and IlvC that can be related to the protection against oxidative stress events. |
| Source | XI Convegno Nazionale di Biotecnologia, Varese, 27-29 giugno 2012 |
| Keywords | Rhodanese-like proteinsRhdAA. vinelandiiOxidative stressIlvCPull-down approaches |
| Year | 2012 |
| Type | Poster |
| Authors | William Remelli; Morena Seregni; Nicoletta Guerrieri, Fabio Forlani |
| Text | 329713 2012 Rhodanese like proteins RhdA A. vinelandii Oxidative stress IlvC Pull down approaches Identification of protein partners of the Azotobacter vinelandii rhodanese like protein RhdA by pull down approaches William Remelli; Morena Seregni; Nicoletta Guerrieri, Fabio Forlani CNR ISE; Dipartimento di Scienze per gli Alimenti, la Nutrizione e l Ambiente, Universita degli Studi di Milano, Milano Rhodaneses TST; EC 2.8.1.1 catalyze in vitro the transfer of sulfane sulfur from thiosulfate to cyanide with the concomitant formation of thiocyanate. Genome sequence analyses evidenced the presence of more than 14000 sequences coding for putative rhodanese like proteins RDPs . These sequences are distributed in all taxa thus suggesting RDPs involvement in biological processes different from cyanide detoxification. Studies aiming to unravel RDP biological functions highlighted the relationship between members of this superfamily and the maintenance of the intracellular redox homeostasis. This ability may rely in the peculiar RDP catalytic domain that consists of a cysteine residue centered in an electropositive environment that promotes the stabilization of the bio active persulfide sulfur. The aim of this work was to gain more insights about RDP biological function by the identification of protein interaction partners. For this reason we used tagged recombinant versions of the biochemically characterized RDP RhdA from Azotobacter vinelandii, as a bait to isolate interaction partners by pull down approaches. We identified IlvC, an oxidative sensitive ketol acid reductoisomerase KARI; EC 1.1.1.86 . The partial inhibition of KARI activity in the A. vinelandii RhdA null mutant strain suggests a functional interaction between RhdA and IlvC that can be related to the protection against oxidative stress events. Published version XI Convegno Nazionale di Biotecnologia Varese 27 29 giugno 2012 Internazionale Contributo Poster 2012_Poster_CNBXI.pdf Poster nicoletta.guerrieri GUERRIERI NICOLETTA TA.P04.016.004 Ecologia teorica e applicata degli ecosistemi acquatici |