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. 2019 Dec 2;9(12):815. doi: 10.3390/biom9120815

Figure 3.

Figure 3

ClpG has higher disaggregation activity towards complex aggregates. (a) Soluble 3H-labeled proteins from an E. coli ΔclpB cell lysate (including Luciferase) were heat shocked to 46 °C for 15 min. Protein aggregates were isolated by centrifugation and resuspended in buffer. Disaggregase activities were monitored by determining the amount of solubilized 3H-labeled proteins (b,c) or Luciferase refolding (d,e). Disaggregation reactions with ClpB and ClpB-K476C included the cooperating DnaK system. Luciferase activities before heat shock were set to 100%. Rates of protein solubilization (c) and Luciferase reactivation (e) were determined. Standard deviations are given (n = 3).