Efficient signal transduction by a chimeric yeast-mammalian G protein alpha subunit Gpa1-Gsalpha covalently fused to the yeast receptor Ste2
作者： R. Medici
关键词: Biology 、 Gs alpha subunit 、 Cell biology 、 Saccharomyces cerevisiae 、 Fusion protein 、 Receptor 、 Biochemistry 、 Signal transduction 、 G protein 、 Protein subunit 、 G alpha subunit
摘要: Saccharomyces cerevisiae uses G protein-coupled receptors for signal transduction. We show that a fusion protein between the alpha-factor receptor (Ste2) and Galpha subunit (Gpa1) transduces efficiently in yeast cells devoid of endogeneous STE2 GPA1 genes. To evaluate function different domains Galpha, chimera N-terminal region Gpa1 C-terminal rat Gsalpha has been constructed. This chimeric Gpa1-Gsalpha is capable restoring viability to haploid gpa1Delta cells, but transduction prevented. consistent with evidence showing C-terminus homologous required receptor-G recognition. Surprisingly, Ste2 able transduce efficiently. It appears, therefore, mainly responsible bringing into close proximity receptor's intracellular domains, thus ensuring efficient coupling, rather than having particular role transmitting signal. confirm this conclusion, we two proteins interacting each other (such as Snf1 Snf4, or Ras Raf), them fused either allow
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