D. Jenness

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STE2 encodes a component of the S. cerevisiae alpha-pheromone receptor that is essential for induction of physiological changes associated with mating. Analysis of C-terminal truncation mutants of STE2 demonstrated that the essential sequences for ligand binding and signal transduction are included within a region containing seven putative transmembrane(More)
The division cycle of yeast a cells is inhibited by alpha-factor. Haploid a cells were found to bind 35S-labeled alpha-factor, whereas haploid alpha cells and diploid a/alpha cells showed little binding. The association of alpha-factor with a cells was reversible upon dilution. Unlabeled alpha-factor competed for binding of 35S-alpha-factor; the(More)
The alpha factor pheromone inhibits the division of yeast a cells. A general method was developed for isolating mutants that exhibit constitutive activation of the pheromone response pathway. A dominant allele of the STE4 locus was recovered in addition to recessive mutations in the SCG1 gene. SCG1 and STE4 are known to encode G alpha and G beta homologs,(More)
The peptide pheromone, alpha-factor, was found to elicit down regulation of receptor sites on yeast a cell targets. Cellular uptake of alpha-factor accompanied the loss of receptor sites. Receptor-deficient a cells bearing a deletion of the STE2 gene were unable to internalize alpha-factor. Cultures were found to reaccumulate receptor sites following the(More)
even when did not believe in myself and my family for an upbringing that encouraged me to follow my dreams and whose constant support helped me achieve this goal. ACKNOWLEDGMENTS I gratefully thank Bob Lahue for being all the things that a mentor should be: a knowledgeable and talented scientist, a patient and caring teacher and, when he needed to be, an(More)
This study investigates endocytosis of Saccharomyces cerevisiae α-factor receptor and the role that receptor oligomerization plays in this process. α-factor receptor contains signal sequences in the cytoplasmic C-terminal domain that are essential for ligand-mediated endocytosis. In an endocytosis complementation assay, we found that oligomeric complexes of(More)
The interaction between ribosomal proteins of the 30s subunit with intact 50s subunits was investigated. Experiments with mixtures of total 30s proteins indicated that several 30s proteins including protein s4 would form a stable complex with 50s subunits. Further work with pure s4 indicates that this protein binds stoichiometrically to the 50s subunits,(More)
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