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Fig. 3 | Biology Direct

Fig. 3

From: Models of buffering of dosage imbalances in protein complexes

Fig. 3

Buffer effect in the steady-state. a Realistic model in which synthesis of both A and B is considered along with their degradation and that of the dimer (upper panel). The lower panels represent the buffering response of heterodimer AB formation to changing the parameter DADB/kAB. For the “normal” conditions, the parameters were: SA = SB = 1nM/min, DA = DB = 0.01 min−1 and kAB ranged from 0.000001 to 1. Here kAB = 0 because the assembly was considered to be irreversible. The ordinates represent the % of AB when either SA or SB is changed (0.5X or 1.5X) with respect to SA = SB. The results were obtained using equation 1. In such conditions when MPC = DADB/kAB ranges from SA/5 to SA/4 there is maximum buffering for deletions. As discussed in the text, the findings obtained here hold for a reversible situation (only the mathematical expression of the MPC changes). b Buffering response of the heterodimer AB formation to changing SB (as if it varied in a population). As above, SA = 1 and the ratio DADB/kAB = 0.25. The span of the SB values induces a (small) variation of at most 25 % of AB production in any direction with respect to SA = SB = 1nM/min. c Buffering response of heterodimer AB formation to changing DB (as if it varied in a population). As above, kAB = 0.0004 and DA = 0.01. SA = SB = 1nM/min. The span of the DB values displayed induces a maximum decrease of 25 % of AB production with respect to DA = DB = 0.01 min−1

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