Póster: Rosario "Ciudad Candia"

El objetivo general es visibilizar la producción de la empresa, que permitirá realizar un recorrido transversal en el desarrollo arquitectónico local, hilvanando períodos históricos, proyectistas y técnicas constructivas. Es notable como en la historiografía de la arquitectura prevalece la cita del proyectista, relegando a un segundo plano los hacedores que contribuyeron con su saber empírico y fáctico a la construcción de la ciudad.Fil: Secretaria de Ciencia y Tecnología - Universidad Nacional de Rosario. Facultad de Arquitectura, Planeamiento y Diseño; Argentina

Yeast Genes Controlling Responses to Topogenic Signals in a Model Transmembrane Protein

Yeast protein insertion orientation (PIO) mutants were isolated by selecting for growth on sucrose in cells in which the only source of invertase is a C-terminal fusion to a transmembrane protein. Only the fraction with an exocellular C terminus can be processed to secreted invertase and this fraction is constrained to 2–3% by a strong charge difference signal. Identified pio mutants increased this to 9–12%. PIO1 is SPF1, encoding a P-type ATPase located in the endoplasmic reticulum (ER) or Golgi. spf1-null mutants are modestly sensitive to EGTA. Sensitivity is considerably greater in an spf1 pmr1 double mutant, although PIO is not further disturbed. Pmr1p is the Golgi Ca(2+) ATPase and Spf1p may be the equivalent ER pump. PIO2 is STE24, a metalloprotease anchored in the ER membrane. Like Spf1p, Ste24p is expressed in all yeast cell types and belongs to a highly conserved protein family. The effects of ste24- and spf1-null mutations on invertase secretion are additive, cell generation time is increased 60%, and cells become sensitive to cold and to heat shock. Ste24p and Rce1p cleave the C-AAX bond of farnesylated CAAX box proteins. The closest paralog of SPF1 is YOR291w. Neither rce1-null nor yor291w-null mutations affected PIO or the phenotype of spf1- or ste24-null mutants. Mutations in PIO3 (unidentified) cause a weaker Pio phenotype, enhanced by a null mutation in BMH1, one of two yeast 14-3-3 proteins