Computational study of a budding yeast model of Tyson and Novák

2014 ◽  
Vol 96 ◽  
pp. 207-223 ◽  
Author(s):  
Willy Govaerts ◽  
Charlotte Sonck
Keyword(s):  
Budding Yeast ◽  
Computational Study ◽  
Yeast Model

α-Synuclein Budding Yeast Model: Toxicity Enhanced by Impaired Proteasome and Oxidative Stress

2006 ◽  
Vol 28 (2) ◽  
pp. 161-178 ◽  
Author(s):  
Nijee Sharma ◽  
Katrina A. Brandis ◽  
Sara K. Herrera ◽  
Brandon E. Johnson ◽  
Tulaza Vaidya ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Budding Yeast ◽  
And Oxidative Stress ◽  
Yeast Model

scholarly journals A Budding Yeast Model for Human Disease Mutations in the EXOSC2 Cap Subunit of the RNA Exosome

RNA ◽  
2021 ◽  
pp. rna.078618.120
Author(s):  
Maria C Sterrett ◽  
Liz Enyenihi ◽  
Sara W Leung ◽  
Laurie Hess ◽  
Sarah E Strassler ◽  
...  
Keyword(s):  
Human Disease ◽  
Budding Yeast ◽  
Disease Mutations ◽  
Rna Exosome ◽  
Yeast Model

scholarly journals A Budding Yeast Model and Screen to Define the Functional Consequences of Oncogenic Histone Missense Mutations

2021 ◽  
Author(s):  
Laramie D. Lemon ◽  
Sneha Kanna ◽  
Kim Wai Mo ◽  
Miranda Adams ◽  
Haley Choi ◽  
...  
Keyword(s):  
Rna Binding ◽  
Budding Yeast ◽  
Dominant Negative ◽  
Missense Mutations ◽  
Cyclin Dependent Kinase ◽  
Histone H4 ◽  
Functional Consequences ◽  
Lysine Acetyltransferase ◽  
Mutant Cells ◽  
Yeast Model

Somatic missense mutations in histone genes turn these essential proteins into oncohistones, which can drive oncogenesis. Understanding how missense mutations alter histone function is challenging in mammals as the changes occur in a single histone gene. For example, described oncohistone mutations predominantly occur in the histone H3.3 gene, despite the human genome encoding 15 H3 genes. To understand how oncogenic histone missense mutations alter histone function, we leverage the budding yeast model, which encodes only two H3 genes, to explore the functional consequences of oncohistones H3K36M, H3G34W, H3G34L, H3G34R, and H3G34V. An analysis of cells that express each of these variants as the sole copy of H3 reveals that H3K36-mutants show different drug sensitivities compared to H3G34 mutants. This finding suggests that changes to proximal amino acids in the H3 N-terminal tail alter distinct biological pathways. We exploited the caffeine sensitive growth of H3K36 mutant cells to perform a high copy suppressor screen. This screen identified genes linked to histone function and transcriptional regulation, the histone H4/H2A acetyltransferase, Esa1, a forkhead-associated domain-containing gene expression regulator, Tos4, an m6A RNA binding protein, Pho92, and a cyclin-dependent kinase, Sgv1/Bur1. We show that the Esa1 lysine acetyltransferase activity is critical for suppression of the caffeine sensitive growth of H3K36R mutant cells while neither of the characterized binding interactions of Tos4 nor Pho92 are required for suppression. Finally, Sgv1/Bur1-mediated suppression may occur through a dominant negative mechanism. This screen identifies pathways that could be altered by oncohistone mutations and highlights the value of yeast genetics to identify pathways altered by such mutations.

Ultrastructure of the effect of T-514 obtained from Karwinskia humboldtiana on assembly and integrity of yeast's peroxisomes

1991 ◽  
Vol 49 ◽  
pp. 136-137
Author(s):  
J. Sepulveda-Saavedra ◽  
I. Vander-Klei ◽  
M. Venhuis ◽  
Y. Piñeyro-Lopez
Keyword(s):  
Culture Conditions ◽  
Toxic Effects ◽  
Candida Boidinii ◽  
Central Mexico ◽  
Poisonous Plant ◽  
Biological Behaviour ◽  
Enzyme Content ◽  
Fat Deposits ◽  
Yeast Model

Karwinskia humboldtiana is a poisonous plant that grows in semi desertic areas in north and central México. It produces several substances with different toxic effects. One of them designated T-514 damages severely the lung, kidney and liver, producing in the hepatoeyte large intracellular fat deposits and necrosis. Preliminary observations demonstrated that three is a decrease in the amount of peroxisomes in the hepatocytes of experimentally intoxicated rats and monkeys. To study the effect exerted by the T-514 on peroxisomes, a yeast model was selected, thus, three species: Saccha romices cerevisiae, Ilansenula polymorpha and Candida boidinii were used, because there is information concerning their peroxisome's morphology, enzyme content, biological behaviour under different culture conditions and biogenesis.

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