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The PHO84 gene of Saccharomyces cerevisiae encodes an inorganic phosphate transporter.
TLDR
Hydropathy analysis suggested that the secondary structure of the PHO84 protein consists of two blocks of six transmembrane domains separated by 74 amino acid residues, and nucleotide sequence predicted a protein of 596 amino acids with a sequence homologous to that of a superfamily of sugar transporters.
Two new genes, PHO86 and PHO87, involved in inorganic phosphate uptake in Saccharomyces cerevisiae
TLDR
These and the other findings suggest that the Pho86p and Pho87p proteins collaborate with Pho84p in Pi uptake, and are suggested to be identical with YCR524, according to the published nucleotide sequence of chromosome III.
Putative GTP-binding protein, Gtr1, associated with the function of the Pho84 inorganic phosphate transporter in Saccharomyces cerevisiae.
TLDR
Recombination between chromosome V and chromosome XIII by using a plasmid-encoded site-specific recombination system indicated that the order of these genes was telomere-TUB3-PHO84-GTR1-CENXIII.
Characterization of a sterol carrier protein 2/3-oxoacyl-CoA thiolase from the cotton leafworm (Spodoptera littoralis): a lepidopteran mechanism closer to that in mammals than that in dipterans.
TLDR
The mRNA expression pattern and the gene structure suggest that SCPx from S. littoralis (a lepidopteran) is evolutionarily closer to that of mammals than to that that of dipterans.
Thiolase involved in bile acid formation.
TLDR
The production of cholic acid and chenodeoxycholic acid from the precursors on incubation with the bifunctional protein and sterol carrier protein x or P-44 was confirmed by gas chromatography.
Structure and distribution of specific cis-elements for transcriptional regulation of PH084 in Saccharomyces cerevisiae
TLDR
Results of expression studies with a CYC1-lacZ fusion gene with various 36-bp oligonucleotides indicated that the 6-bp motif flanked by a thymine nucleotide at its 5′ end is much less effective as a UAS site for Pho4p in vivo than other versions.
Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate.
TLDR
The expression and localization of type-II 3-oxoacyl-CoA thiolase in the nematode Caenorhabditis elegans are examined, suggesting their common physiological roles.
A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis elegans, which is similar to sterol carrier protein x but lacks the sequence of sterol carrier protein 2.
TLDR
It is concluded that nematode P-44 and mammalian SCPx constitute a second isoform of thiolase, which the authors propose to term type-II 3-ketoacyl-CoA thiolases.
Predominant localization of non‐specific lipid‐transfer protein of the yeast Candida tropicalis in the matrix of peroxisomes
TLDR
Results are consistent with the view that PXP‐18 is the matrix protein of peroxisomes and must function in a system other than that of lipid transfer.
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