Isocitrate lyase of the yeast Kluyveromyces lactis is subject to glucose repression but not to catabolite inactivation

Curr Genet (2004) 44:305–316

Figure 6, which shows the glucose-induced inactivation of various isocitrate lyases, was omitted from both online and printed version of the article. In addition, the figure citations in the last paragraph of the Results section should read “Fig. 6A, Fig. 6B ... Fig. 6F”. Fig. 6 is shown below.

Fig. 6A-F

Catabolite inactivation kinetics of isocitrate lyase and fructose 1,6-bisphosphatase. Wild-type strains were pregrown on SCD and transformants on SCDura or SCDleu to select for plasmid maintenance. For derepression cells were transferred to YEPE medium and incubated overnight. Inactivation was started by addition of glucose to a final concentration of 2% at time zero to one half of the culture (glucose). The remaining culture was further incubated on YEPE (ethanol). Samples were taken at the times indicated and isocitrate lyase (A, B and C) or fructose 1,6-bisphosphatase (D, E and F) were assayed as described in materials and methods. Designation of yeast strains employed (as transformed with the plasmids indicated): A and D = KB6-2C; B = FMY401 (Scicl1::LEU2); C = KliclΔ13 (Klicl1::HIS3); E = VWHF1 (Scfbp1::LEU2); F = KlfbpΔ1 (Klfbp1::URA3)