Abstract
The HypF protein is involved in the maturation and regulation of hydrogenases. The N-terminal domain of HypF (HypF-N) has served as a key model system to study the pathways of protein amyloid formation and the nature of the toxicity of pre-fibrilar protein oligomers. This domain can aggregate into two forms of oligomers having significantly different toxic effects when added to neuronal cultures. Here, NMR assignments of HypF-N backbone resonances are presented in its native state and under the conditions favouring the formation of toxic and non-toxic oligomers. The analyses of chemical shifts provide insights into the protein conformational state and the possible pathways leading to the formation of different types of oligomers.
Highlights
HypF plays a chaperone role in the biogenesis of nickel–iron [NiFe] insertion in hydrogenase enzymes from E. coli (Maier and Böck 1996)
HypF-N has unique features to enable the elucidation of the molecular basis of the toxicity of protein oligomers, as it can form two different types of protein oligomers that, while being similar in composition, shape, size and morphology, have significantly different toxic effects when incubated with cellular cultures, with only one showing toxic effects
In the present work we present a detailed characterisation of the general structural properties of HypF-N in its native state and under the two oligomerising conditions
Summary
HypF plays a chaperone role in the biogenesis of nickel–iron [NiFe] insertion in hydrogenase enzymes from E. coli (Maier and Böck 1996). Despite the relevance of this protein in the context of amyloid diseases, the assignments of the NMR resonances of HypF-N under the conditions A and B, which respectively generate toxic and non-toxic oligomers, are not available from the BMRB. In the present work we present a detailed characterisation of the general structural properties of HypF-N in its native state and under the two oligomerising conditions.
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