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Stabilization of the “open” conformer of apoIscU on the surface of polystyrene nanobeads accelerates assembly of a 2Fe2S structure

100%

Barbiroli A., Bonomi F., Iametti S., Marengo M.

vol. 2

issue 1

The scaffold protein IscU is involved in the assembly/transfer of FeS clusters. IscU exists in both open and closed conformation. The clusterless open conformation of IscU adheres to the hydrophobic surface of polystyrene nanobeads, as observed for other proteins. Increased accessibility of the ligand cysteines in bound IscU facilitates assembly of a 2Fe2S cluster, and the cluster-bearing structured form of IscU does not interact with the nanobeads, thus ensuring turnover. The dependence of accelerated cluster assembly on the nanobeads concentration pointed to steric and crowding effects as for promoting cluster formation, and confirms the requirement for structural flexibility of IscU .

Cysteine-containing peptides are produced by sequential clipping, but not released, from lupin 11S storage globulin during early germination

88%

Capraro J., Galanti E., Marengo M., Duranti M., Scarafoni A.

vol. 2

issue 1

The digestion of the seed storage proteins is a finely regulated process operated by several proteases whose action is influenced by the exposure of specific regions, which became progressively available upon their action. We focused our study on the initial stages of germination, where more subtle modifications to the storage proteins are expected. Small-size peptides containing cysteine residues and other possible metalbinding regions are de facto produced but are not released from the “parental” protein since they remain bound trough disulphide bridges. The meaning of these findings is discussed.

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2 Peptidomics

2 2016

2 Marengo M.

1 Barbiroli A.

1 Bonomi F.

1 Capraro J.

1 Duranti M.

1 Galanti E.

1 Iametti S.

1 Scarafoni A.

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Stabilization of the “open” conformer of apoIscU on the surface of polystyrene nanobeads accelerates assembly of a 2Fe2S structure

Cysteine-containing peptides are produced by sequential clipping, but not released, from lupin 11S storage globulin during early germination