文摘
14-3-3 proteins form a family of conserved eukaryotic proteins binding to over 200 different proteinsinvolved in nearly all cellular processes. The yeast Saccharomyces cerevisiae has two genes encoding14-3-3 proteins, BMH1 and BMH2. As 14-3-3 proteins are essential in most S. cerevisiae strains, weconstructed a bmh mutant with suboptimal 14-3-3 protein activity. Here, we report the effect of thesebmh mutations on the proteome as determined by two-dimensional gel electrophoresis and massspectrometry. We identified 26 proteins of which the levels increased by more than 2.0-fold and 51proteins of which the levels decreased by more than 2.0-fold in the bmh mutant compared with thoseof the wild-type strain. For only 9 of these proteins, a more than 2.0-fold alteration was found at thetranscriptional level. The levels of many proteins involved in gluconeogenesis, including Fba1, Eno1,Eno2, Tpi1, Pck1, Mdh2, Tdh2, Tdh3, and Gpm1, increased in the mutant, whereas the levels of severalproteins involved in amino acid biosynthesis and translation and heat shock proteins were lower. Ourstudies indicate that 14-3-3 proteins control the S. cerevisiae proteome at the post-transcriptional level,in agreement with the binding of 14-3-3 proteins to proteins involved in protein synthesis anddegradation. In addition, our studies suggest a key role in the regulation of carbohydrate metabolismby 14-3-3 proteins.