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Abstract
SlyD is a two domain protein shown to have many and varied roles in E. coli cell physiology. Recently, SlyD has been show to be important for hydrogenase maturation. H. pylori has a homolog of the SlyD protein. To investigate the role of the whole protein and two domains of SlyD in hydrogenase maturation, I created two mutant strains, one lacking the full gene (slyD) and one lacking only the C-terminal domain (mbd). I also purified SlyD to use in crosslinking studies. The slyD mutant strain had a 60% decrease in hydrogenase activity and the mbd mutant strain had a 30% decrease as compared to the wildtype. Nickel complementation in the growth media was unable to cure the strains. Purified H. pylori SlyD was unable to crosslink with HypB suggesting that SlyD probably affects the hydrogenase maturation pathway differently than in E. coli.