Elda gráfico : revista ilustrada: Año 1 Número 1 - 6 septiembre 1928

número procedente del Ayto. Elda

1.6 Lloyd Gaines, Valedictorian, Vashon Class of 1931

Lloyd Gaines also helped to support his family by selling magazine subscriptions. He graduated in 1931 after only three years and served as the Valedictorian of his class. As a senior, Gaines finished first in a local essay contest, winning a prize of $250 (equivalent to $3000 in modern currency) that he used to enroll as a student at Stowe Teachers College in St. Louis for the 1931-32 school year

1.6 Lloyd Hogsett, University of Missouri Legal Counsel

By March, 1936, the University of Missouri formally rejected Gaines because Missouri law would not permit a person of African descent to enter a white school. Within three weeks, the NAACP petitioned the court asking the University of Missouri to open its doors to Gaines on the grounds that it was the only public law school in Missouri.

The Role of Glucosidase I (Cwh41p) in the Biosynthesis of Cell Wall β-1,6-Glucan Is Indirect

CWH41, a gene involved in the assembly of cell wall β-1,6-glucan, has recently been shown to be the structural gene for Saccharomyces cerevisiae glucosidase I that is responsible for initiating the trimming of terminal α-1,2-glucose residue in the N-glycan processing pathway. To distinguish between a direct or indirect role of Cwh41p in the biosynthesis of β-1,6-glucan, we constructed a double mutant, alg5Δ (lacking dolichol-P-glucose synthase) cwh41Δ, and found that it has the same phenotype as the alg5Δ single mutant. It contains wild-type levels of cell wall β-1,6-glucan, shows moderate underglycosylation of N-linked glycoproteins, and grows at concentrations of Calcofluor White (which interferes with cell wall assembly) that are lethal to cwh41Δ single mutant. The strong genetic interactions of CWH41 with KRE6 and KRE1, two other genes involved in the β-1,6-glucan biosynthetic pathway, disappear in the absence of dolichol-P-glucose synthase (alg5Δ). The triple mutant alg5Δcwh41Δkre6Δ is viable, whereas the double mutant cwh41Δkre6Δ in the same genetic background is not. The severe slow growth phenotype and 75% reduction in cell wall β-1,6-glucan, characteristic of the cwh41Δkre1Δ double mutant, are not observed in the triple mutant alg5Δcwh41Δkre1Δ. Kre6p, a putative Golgi glucan synthase, is unstable in cwh41Δ strains, and its overexpression renders these cells Calcofluor White resistant. These results demonstrate that the role of glucosidase I (Cwh41p) in the biosynthesis of cell wall β-1,6-glucan is indirect and that dolichol-P-glucose is not an intermediate in this pathway.