Structure and Function of the Subunits of the Vacuolar Membrane H+-ATPase of Saccharomyces Cerevisiae

1987 ◽  
pp. 173-178
Author(s):  
Yasuhiro Anraku ◽  
Etsuko Uchida ◽  
Yoshinori Ohsumi
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Structure And Function ◽  
Vacuolar Membrane ◽  
And Function

scholarly journals The Schizosaccharomyces pombe cho1+ Gene Encodes a Phospholipid Methyltransferase

Genetics ◽  
1998 ◽  
Vol 150 (2) ◽  
pp. 553-562
Author(s):  
Margaret I Kanipes ◽  
John E Hill ◽  
Susan A Henry
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Sequence Analysis ◽  
Schizosaccharomyces Pombe ◽  
Gene Disruption ◽  
Structure And Function ◽  
Biosynthetic Enzyme ◽  
Gene Encoding ◽  
Complementation Groups ◽  
Eukaryotic Organisms ◽  
And Function

Abstract The isolation of mutants of Schizosaccharomyces pombe defective in the synthesis of phosphatidylcholine via the methylation of phosphatidylethanolamine is reported. These mutants are choline auxotrophs and fall into two unlinked complementation groups, cho1 and cho2. We also report the analysis of the cho1+ gene, the first structural gene encoding a phospholipid biosynthetic enzyme from S. pombe to be cloned and characterized. The cho1+ gene disruption mutant (cho1Δ) is viable if choline is supplied and resembles the cho1 mutants isolated after mutagenesis. Sequence analysis of the cho1+ gene indicates that it encodes a protein closely related to phospholipid methyltransferases from Saccharomyces cerevisiae and rat. Phospholipid methyltransferases encoded by a rat liver cDNA and the S. cerevisiae OPI3 gene are both able to complement the choline auxotrophy of the S. pombe cho1 mutants. These results suggest that both the structure and function of the phospholipid N-methyltransferases are broadly conserved among eukaryotic organisms.

scholarly journals Structure-function analysis of Arabidopsis TOPLESS reveals fundamental conservation of repression mechanisms across eukaryotes

2020 ◽  
Author(s):  
Alexander R. Leydon ◽  
Wei Wang ◽  
Hardik P. Gala ◽  
Sabrina Gilmour ◽  
Samuel Juarez-Solis ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Function Analysis ◽  
Structure And Function ◽  
Environmental Cues ◽  
Auxin Response ◽  
Middle Domain ◽  
N Terminus ◽  
And Function ◽  
The Relationship ◽  
Repression Domain

SummaryThe plant corepressor TOPLESS (TPL) is recruited to a large number of loci that are selectively induced in response to developmental or environmental cues, yet the mechanisms by which it inhibits expression in the absence of these stimuli is poorly understood. Previously, we had used the N-terminus of Arabidopsis thaliana TPL to enable repression of a synthetic auxin response circuit in Saccharomyces cerevisiae (yeast). Here, we leveraged the yeast system to interrogate the relationship between TPL structure and function, specifically scanning for repression domains. We identified a potent repression domain in Helix 8 located within the CRA domain, which directly interacted with the Mediator middle domain subunits Med21 and Med10. Interactions between TPL and Mediator were required to fully repress transcription in both yeast and plants. In contrast, we found that multimer formation, a conserved feature of many corepressors, had minimal influence on the repression strength of TPL.

scholarly journals Repression by the Arabidopsis TOPLESS corepressor requires association with the core Mediator complex

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Alexander R Leydon ◽  
Wei Wang ◽  
Hardik P Gala ◽  
Sabrina Gilmour ◽  
Samuel Juarez-Solis ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Structure And Function ◽  
Mediator Complex ◽  
Environmental Cues ◽  
Auxin Response ◽  
The Core ◽  
N Terminus ◽  
And Function ◽  
The Relationship ◽  
Repression Domain

The plant corepressor TOPLESS (TPL) is recruited to a large number of loci that are selectively induced in response to developmental or environmental cues, yet the mechanisms by which it inhibits expression in the absence of these stimuli is poorly understood. Previously, we had used the N-terminus of Arabidopsis thaliana TPL to enable repression of a synthetic auxin response circuit in Saccharomyces cerevisiae (yeast). Here, we leveraged the yeast system to interrogate the relationship between TPL structure and function, specifically scanning for repression domains. We identified a potent repression domain in Helix 8 located within the CRA domain, which directly interacted with the Mediator middle module subunits Med21 and Med10. Interactions between TPL and Mediator were required to fully repress transcription in both yeast and plants. In contrast, we found that multimer formation, a conserved feature of many corepressors, had minimal influence on the repression strength of TPL.

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