Figure 4: The in vitro characterization of RdlB mutant aggregation. | Scientific Reports

Figure 4: The in vitro characterization of RdlB mutant aggregation.

From: The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolor

Figure 4

(A) Aggregation of RdlB and its mutants monitored by ThT fluorescence intensity. All conditions were identical and all protein concentrations 10 μM. (B) In vitro self-polymerization of three synthetic peptides based on the N-terminal sequence of RdlB monitored by ThT fluorescence. The peptide concentration was 40 μM. (A,B) Readings were taken every 3 min in a FLUOstar Omega microplate reader with 700 rpm orbital shaking. (C,D) Negatively stained electron micrograph of aggregates formed by RdlB peptide fragments after incubation for 4 days. Scale bars are 100 nm. (C) Peptide corresponding to residues 11–27 of RdlB (NGNGASQYFGNSMTTGN). Fibrils appear as short, rigid rods. (D) Peptide corresponding to residues 28–42 of RdlB (MSPQMALIQGSFNKP). Fibrils appear significantly shorter and thinner, the morphology of these fibrils appears more fragile as shreds of fibrils were often observed indicating fragmentation.

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