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. 2007 Sep;145(1):41–48. doi: 10.1104/pp.107.104000

Figure 6.

Figure 6.

Lipoylation of the PDH and KGDH E2 subunits is partially mtKAS dependent in leaves, but mtKAS independent in roots. A, Lipoylation of the mitochondrial E2 subunits of PDH and KGDH is reduced to a much lesser extent than that of H protein. B, Lipoylation of H protein in mitochondrial extracts is detectable only after strong overexposure of the immunoblots. C, The content of unlipoylated H protein remains unchanged. D, Lipoylation of the PDH and KGDH E2 subunits is independent on mtKAS in roots. For these experiments, 3 μg mitochondrial protein (A–C) or 5 μg of root soluble protein (D) of high CO2-grown wild-type (WT), mtkas-1 (-1), and mtkas-2 (-2) plants were loaded per slot of a 12% SDS-polyacrylamide gel. A picture of the complete gel from D is available in the online version of this article as Supplemental Figure S4.