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. 2011 Mar;79(6):1574–1593. doi: 10.1111/j.1365-2958.2011.07542.x

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Copyright © 2011 Blackwell Publishing Ltd

Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.

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Fig. 7 — Many C. albicans proteins are ubiquitinated in a polyubiquitin-dependent fashion.A. Protein ubiquitination in wild-type C. albicans cells under different stress conditions. C. albicans THE1 was grown for 5 h and then exposed to the specified stress for 1 h (Experimental procedures). Protein extracts were prepared and analysed by Western blotting with an α-ubiquitin antibody.B. Impact of UBI4 inactivation upon protein ubiquitination in C. albicans. UBI4/UBI4 (THE1), UBI4/ubi4 (MLC35) and ubi4/ubi4 (MLC40) cells were grown for 5 h and then stressed for 1 h with heat or peroxide (Experimental procedures). Protein extracts were prepared and analysed by Western blotting. To control for loading, membranes were stripped and reprobed for Hsp90. Closed arrows highlight bands observed in wild-type cells that are absent following UBI4 inactivation, and the open arrow indicates a band observed in heat stressed cells that is absent in the ubi4/ubi4 mutant. The bracket indicates numerous ubiquitinated proteins, the levels of which are decreased in ubi4/ubi4 cells.C. Quantification of protein levels in the heterozygous UBI4/ubi4 (MLC35) and null ubi4/ubi4 (MLC40) strains under the three conditions tested.