Expression of the cloned uracil permease gene of Saccharomyces cerevisiae in a heterologous membrane.

Chevallier, M. R.; Lacroute, François

doi:10.1002/j.1460-2075.1982.tb01177.x

Cited by 16 publications

(15 citation statements)

References 14 publications

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“…Also known as purine-related transporters, they generally transport purines in a proton symport mode and consist of 12 transmembrane domains (TMs; Saier et al, 2009; www.tcdb.org). The uridine transporter FUI1 and the uracil transporter FUR4 from Saccharomyces cerevisiae (Chevallier and Lacroute, 1982; Zhang et al, 2006), the benzyl-hydantoin transporter MHP1 from Microbacterium liquefaciens (Weyand et al, 2008) and the cytosine- purine transporter FCYB from Aspergillus nidulans (Krypotou et al, 2012) are examples for well-studied NCS1 proteins.…”

Section: The Nucleobase:cation Symporter 1 Familymentioning

confidence: 99%

Nucleobase and nucleoside transport and integration into plant metabolism

et al. 2014

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Nucleotide metabolism is an essential process in all living organisms. Besides newly synthesized nucleotides, the recycling (salvage) of partially degraded nucleotides, i.e., nucleosides and nucleobases serves to keep the homeostasis of the nucleotide pool. Both types of metabolites are substrates of at least six families of transport proteins in Arabidopsis thaliana (Arabidopsis) with a total of 49 members. In the last years several members of such transport proteins have been analyzed allowing to present a more detailed picture of nucleoside and nucleobase transport and the physiological function of these processes. Besides functioning in nucleotide metabolism it turned out that individual members of the before named transporters exhibit the capacity to transport a wide range of different substrates including vitamins and phytohormones. The aim of this review is to summarize the current knowledge on nucleobase and nucleoside transport processes in plants and integrate this into nucleotide metabolism in general. Thereby, we will focus on those proteins which have been characterized at the biochemical level.

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Section: The Nucleobase:cation Symporter 1 Familymentioning

confidence: 99%

Nucleobase and nucleoside transport and integration into plant metabolism

et al. 2014

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“…Yeast cells import uracil via the nucleobase permease FUR4 to support pyrimidine nucleotide salvage (Chevallier and Lacroute, 1982;Jund et al, 1988;Mitterbauer et al, 2002). FUR4 belongs to the Nucleobase:Cation Symporter1 (NCS1) family of transport proteins, also known as purine-related transporters (Saier et al, 2009;www.tcdb.org).…”

Section: Biochemical Characterization Of Pluto a Nucleobase Transpormentioning

confidence: 99%

De Novo Pyrimidine Nucleotide Synthesis Mainly Occurs outside of Plastids, but a Previously Undiscovered Nucleobase Importer Provides Substrates for the Essential Salvage Pathway in Arabidopsis

et al. 2012

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Nucleotide de novo synthesis is highly conserved among organisms and represents an essential biochemical pathway. In plants, the two initial enzymatic reactions of de novo pyrimidine synthesis occur in the plastids. By use of green fluorescent protein fusions, clear support is provided for a localization of the remaining reactions in the cytosol and mitochondria. This implies that carbamoyl aspartate, an intermediate of this pathway, must be exported and precursors of pyrimidine salvage (i.e., nucleobases or nucleosides) are imported into plastids. A corresponding uracil transport activity could be measured in intact plastids isolated from cauliflower (Brassica oleracea) buds. PLUTO (for plastidic nucleobase transporter) was identified as a member of the Nucleobase:Cation-Symporter1 protein family from Arabidopsis thaliana, capable of transporting purine and pyrimidine nucleobases. A PLUTO green fluorescent protein fusion was shown to reside in the plastid envelope after expression in Arabidopsis protoplasts. Heterologous expression of PLUTO in an Escherichia coli mutant lacking the bacterial uracil permease uraA allowed a detailed biochemical characterization. PLUTO transports uracil, adenine, and guanine with apparent affinities of 16.4, 0.4, and 6.3 mM, respectively. Transport was markedly inhibited by low concentrations of a proton uncoupler, indicating that PLUTO functions as a proton-substrate symporter. Thus, a protein for the absolutely required import of pyrimidine nucleobases into plastids was identified.

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“…Yeast uracil permease (UP), encoded by the FUR4 gene, is a plasma membrane protein required for the uptake of uracil (Chevallier, 1982;Chevallier and Lacroute, 1982). A mutated form of the uracil permease, Fur4 -430Np, referred to herein as UP*, contains a 3 amino acid residue insertion in a predicted cytoplasmic loop.…”

Section: Up*: a Quality Control Substratementioning

confidence: 99%

HRDGene Dependence of Endoplasmic Reticulum-associated Degradation

Wilhovsky

Gardner

Hampton

2000

MBoC

101

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Work from several laboratories has indicated that many different proteins are subject to endoplasmic reticulum (ER) degradation by a common ER-associated machinery. This machinery includes ER membrane proteins Hrd1p/Der3p and Hrd3p and the ER-associated ubiquitinconjugating enzymes Ubc7p and Ubc6p. The wide variety of substrates for this degradation pathway has led to the reasonable hypothesis that the HRD (Hmg CoA reductase degradation) gene-encoded proteins are generally involved in ER protein degradation in eukaryotes. We have tested this model by directly comparing the HRD dependency of the ER-associated degradation for various ER membrane proteins. Our data indicated that the role of HRD genes in protein degradation, even in this highly defined subset of proteins, can vary from absolute dependence to complete independence. Thus, ER-associated degradation can occur by mechanisms that do not involve Hrd1p or Hrd3p, despite their apparently broad envelope of substrates. These data favor models in which the HRD gene-encoded proteins function as specificity factors, such as ubiquitin ligases, rather than as factors involved in common aspects of ER degradation. INTRODUCTIONThe endoplasmic reticulum (ER) is an important site of cellular protein degradation in eukaryotes. Both lumenal and integral ER membrane proteins undergo selective degradation for purposes of quality control or feedback regulation (Chun et al., 1990;Klausner and Sitia, 1990). Accordingly, the ER degradation pathway plays an important role in normal and pathological processes, including cholesterol synthesis (Edwards et al., 1983;Nakanishi et al., 1988;Hampton and Rine, 1994), HIV biogenesis (Bour et al., 1995), cystic fibrosis (Jensen et al., 1995;Ward et al., 1995), lipoprotein metabolism (Fisher et al., 1997), and protein quality control (Hiller et al., 1996;Kopito, 1997).ER protein degradation is conserved between yeast and mammals, allowing genetic analysis of this process. In separate studies, yeast mutants deficient in degradation of the normal, ER-resident protein Hmg2p, an isozyme of HMGCoA reductase (HMGR) (Hampton and Rine 1996b), and mutants deficient in ER degradation of CPY*, a misfolded protein that is retained in the lumen of the ER (Knop et al., 1996;Bordallo et al., 1998), have been isolated. The genes from these studies are referred to as HRD (Hmg CoA reductase degradation) and DER (degradation in the endoplasmic reticulum) genes, respectively. For either substrate, ubiquitination is required for subsequent degradation by the proteasome. Ubiquitination is effected by the ER-associated ubiquitin-conjugating enzymes, of which Ubc7p appears to play a major role (Hiller et al., 1996;Hochstrasser, 1996;Hampton and Bhakta, 1997). Furthermore, integral ER membrane proteins Hrd1p/Der3p and Hrd3p are also required for degradation of both of these substrates (Hampton et al., 1996a;Bordallo et al., 1998;Plemper et al., 1999).These and subsequent studies on the HRD/DER genes have indicated a broad role for these genes in the ERassociated ...

show abstract

Expression of the cloned uracil permease gene of Saccharomyces cerevisiae in a heterologous membrane.

Cited by 16 publications

References 14 publications

Nucleobase and nucleoside transport and integration into plant metabolism

Nucleobase and nucleoside transport and integration into plant metabolism

De Novo Pyrimidine Nucleotide Synthesis Mainly Occurs outside of Plastids, but a Previously Undiscovered Nucleobase Importer Provides Substrates for the Essential Salvage Pathway in Arabidopsis

HRDGene Dependence of Endoplasmic Reticulum-associated Degradation

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