scholarly journals Involvement of heme biosynthesis in control of sterol uptake by Saccharomyces cerevisiae.

1985 ◽  
Vol 163 (1) ◽  
pp. 199-207 ◽  
Author(s):  
T A Lewis ◽  
F R Taylor ◽  
L W Parks
Yeast ◽  
2021 ◽  
Author(s):  
Gregory H. Whitaker ◽  
Dustin C. Ernst ◽  
Diana M. Downs

2001 ◽  
Vol 268 (6) ◽  
pp. 1585-1595 ◽  
Author(s):  
Frederique Ness ◽  
Stephane Bourot ◽  
Matthieu Regnacq ◽  
Roberto Spagnoli ◽  
Thierry Berges ◽  
...  

2012 ◽  
Vol 12 (2) ◽  
pp. 244-253 ◽  
Author(s):  
Helen A. Foster ◽  
Mingfei Cui ◽  
Angel Naveenathayalan ◽  
Heike Unden ◽  
Ralf Schwanbeck ◽  
...  

ABSTRACTSut1 is a transcriptional regulator of the Zn(II)2Cys6family in the budding yeastSaccharomyces cerevisiae. The only function that has been attributed to Sut1 is sterol uptake under anaerobic conditions. Here, we show that Sut1 is also expressed in the presence of oxygen, and we identify a novel function for Sut1.SUT1overexpression blocks filamentous growth, a response to nutrient limitation, in both haploid and diploid cells. This inhibition by Sut1 is independent of its function in sterol uptake. Sut1 downregulates the expression ofGAT2,HAP4,MGA1,MSN4,NCE102,PRR2,RHO3, andRHO5. Several of these Sut1 targets (GAT2,HAP4,MGA1,RHO3, andRHO5) are essential for filamentation in haploids and/or diploids. Furthermore, the expression of the Sut1 target genes, with the exception ofMGA1, is induced during filamentous growth. We also show thatSUT1expression is autoregulated and inhibited by Ste12, a key transcriptional regulator of filamentation. We propose that Sut1 partially represses the expression ofGAT2,HAP4,MGA1,MSN4,NCE102,PRR2,RHO3, andRHO5when nutrients are plentiful. Filamentation-inducing conditions relieve this repression by Sut1, and the increased expression of Sut1 targets triggers filamentous growth.


2017 ◽  
Vol 61 (11) ◽  
Author(s):  
Amanpreet Singh ◽  
Ameeta Agarwal ◽  
Yong-jie Xu

ABSTRACT We have previously reported that an erg11 mutation affecting ergosterol synthesis and a hem13 mutation in the heme synthesis pathway significantly sensitize the fission yeast Schizosaccharomyces pombe to hydroxyurea (HU) (1, 2). Here we show that treatment with inhibitors of Erg11 and heme biosynthesis phenocopies the two mutations in sensitizing wild-type cells to HU. Importantly, HU synergistically interacts with the heme biosynthesis inhibitor sampangine and several Erg11 inhibitors, the antifungal azoles, in causing cell lethality. Since the synergistic drug interactions are also observed in the phylogenetically divergent Saccharomyces cerevisiae and the opportunistic fungal pathogen Candida albicans, the synergism is likely conserved in eukaryotes. Interestingly, our genetic data for S. pombe has also led to the discovery of a robust synergism between sampangine and the azoles in C. albicans. Thus, combinations of HU, sampangine, and the azoles can be further studied as a new method for the treatment of fungal infections.


1997 ◽  
Vol 43 (8) ◽  
pp. 792-795 ◽  
Author(s):  
Celestino Di Flumeri ◽  
Nicholas H. Acheson ◽  
Teresa Keng

Uroporphyrinogen decarboxylase catalyzes the fifth step of heme biosynthesis in Saccharomyces cerevisiae. Studies utilizing sulfhydryl-specific reagents suggest that the enzyme requires a cysteine residue within the catalytic site This hypothesis was tested directly by site-directed mutagenesis of highly conserved cysteine-52 to serine or alanine. Plasmids containing these mutations were able to complement a hem6 mutant strain. In addition, properties associated with decreased uroporphyrinogen decarboxylase activity were not detected in the mutant strain transformed with these mutant plasmids. These results suggest that the conserved cysteine-52 by itself is not essential for enzymatic activity.Key words: heme biosynthesis, uroporphyrinogen decarboxylase, site-directed mutagenesis.


Steroids ◽  
1989 ◽  
Vol 53 (3-5) ◽  
pp. 607-623 ◽  
Author(s):  
Dean L. Shinabarger ◽  
George A. Keesler ◽  
Parks Leo W.

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