PcMtr, an aromatic and neutral aliphatic amino acid permease of Penicillium chrysogenum

Trip, Hein; Evers, Melchior E.; Driessen, Arnold J. M.

doi:10.1016/j.bbamem.2004.09.014

Cited by 9 publications

(10 citation statements)

References 31 publications

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“…23-24% identities) to fungal members of the Amino Acid/ Auxin Permease family (TC 2.A.18.4. ), represented by two proteins from Neurospora crassa and Penicillium chrysogenum that have been shown experimentally to transport aromatic and/or neutral amino acids (Koo and Stuart, 1991;Trip et al, 2004). These two latter proteins are located in clade C of the phylogenetic tree ( Figure 1).…”

Section: A Novel Family Of Fungal Dipeptide Transportersmentioning

confidence: 99%

A novel fungal family of oligopeptide transporters identified by functional metatranscriptomics of soil eukaryotes

et al. 2011

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Functional environmental genomics has the potential to identify novel biological functions that the systematic sequencing of microbial genomes or environmental DNA may fail to uncover. We targeted the functions expressed by soil eukaryotes using a metatranscriptomic approach based on the use of soil-extracted polyadenylated messenger RNA to construct environmental complementary DNA expression libraries. Functional complementation of a yeast mutant defective in di/tripeptide uptake identified a novel family of oligopeptide transporters expressed by fungi. This family has a patchy distribution in the Basidiomycota and Ascomycota and is present in the genome of a Saccharomyces cerevisiae wine strain. High throughput phenotyping of yeast mutants expressing two environmental transporters showed that they both displayed broad substrate specificity and could transport more than 60-80 dipeptides. When expressed in Xenopus oocytes one environmental transporter induced currents upon dipeptide addition, suggesting protoncoupled co-transport of dipeptides. This transporter was also able to transport specifically cysteine. Deletion of the two copies of the corresponding gene family members in the genome of the wine yeast strain severely reduced the number of dipeptides that it could assimilate. These results demonstrate that these genes are functional and can be used by fungi to efficiently scavenge the numerous, low concentration, oligopeptides continuously generated in soils by proteolysis.

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Section: A Novel Family Of Fungal Dipeptide Transportersmentioning

confidence: 99%

A novel fungal family of oligopeptide transporters identified by functional metatranscriptomics of soil eukaryotes

et al. 2011

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“…Their uptake is mediated by transmembrane proteins belonging to the specific fungal YAT (TC 2.A.3.10, yeast amino acid transporter) family, a member of the APC (amino acid polyamine choline) superfamily (25), which shows a wide range of substrate specificities and includes representatives in all realms of life (53). In Saccharomyces cerevisiae (51), 18 YAT transporters have been functionally characterized, while only a few have been studied in other organisms (8,25,35,57,67,68,69,72,76; Saccharomyces genome database at http://www.yeastgenome.org/). The YAT family transporters share a common predicted topology, comprising 12 transmembrane domains, and show, even among proteins with completely different substrate specificities, a high degree of sequence identity (2, 25).…”

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confidence: 99%

AgtA, the Dicarboxylic Amino Acid Transporter of Aspergillus nidulans , Is Concertedly Down-Regulated by Exquisite Sensitivity to Nitrogen Metabolite Repression and Ammonium-Elicited Endocytosis

et al. 2009

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We identified agtA, a gene that encodes the specific dicarboxylic amino acid transporter of Aspergillus nidulans. The deletion of the gene resulted in loss of utilization of aspartate as a nitrogen source and of aspartate uptake, while not completely abolishing glutamate utilization. Kinetic constants showed that AgtA is a high-affinity dicarboxylic amino acid transporter and are in agreement with those determined for a cognate transporter activity identified previously. The gene is extremely sensitive to nitrogen metabolite repression, depends on AreA for its expression, and is seemingly independent from specific induction. We showed that the localization of AgtA in the plasma membrane necessitates the ShrA protein and that an active process elicited by ammonium results in internalization and targeting of AgtA to the vacuole, followed by degradation. Thus, nitrogen metabolite repression and ammonium-promoted vacuolar degradation act in concert to downregulate dicarboxylic amino acid transport activity.Amino acids can be utilized by saprophytic fungi as nitrogen and/or carbon sources. Their uptake is mediated by transmembrane proteins belonging to the specific fungal YAT (TC 2.A.3.10, yeast amino acid transporter) family, a member of the APC (amino acid polyamine choline) superfamily (25), which shows a wide range of substrate specificities and includes representatives in all realms of life (53). In Saccharomyces cerevisiae (51), 18 YAT transporters have been functionally characterized, while only a few have been studied in other organisms (8,25,35,57,67,68,69,72,76; Saccharomyces genome database at http://www.yeastgenome.org/). The YAT family transporters share a common predicted topology, comprising 12 transmembrane domains, and show, even among proteins with completely different substrate specificities, a high degree of sequence identity (2, 25). The transporters of the dicarboxylic amino acids glutamate and aspartate have been characterized in S. cerevisiae (DIP5; 47) and Penicillium chrysogenum (PcDIP5; 68) and are members of this family. In A. nidulans, specific dicarboxylic amino acid transport activity and certain aspects of its regulation were previously reported (24, 26, 42, 51, 52), but the corresponding gene(s) was not characterized.In fungi, the genes that encode transporters and enzyme activities involved in nitrogen source utilization are subject to tight transcriptional and/or posttranscriptional controls. Preferred nitrogen sources (such as ammonium and glutamine) repress the transcription of genes involved in the utilization of metabolically less favorable nitrogen sources such as nitrate, purines, or amino acids. In A. nidulans, nitrogen metabolite repression acts by inactivating the AreA GATA transcriptional activator (30) by a number of concurring mechanisms (36, 66). In S. cerevisiae, a transcriptional repression mechanism similar but not identical to the one described above for A. nidulans is operative (see reference 33 for a review).In addition to being subject to transcriptional regulati...

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“…To the best of our knowledge Fpmtr1 is unusual among fungal amino acid transporters in its growth stage specific expression, and its insensitivity to amino acid starvation. Trip et al (2004) suggested that the Mtr-type transporters may be involved in reception of signaling molecules. This hypothesis was based on the low copy number of Mtr homologs found in fungal genomes, as compared to the relative abundance of the AAP transporters in these organisms.…”

Section: Discussionmentioning

confidence: 98%

“…Members of the AAP family share significant sequence similarities and they all contain a typical 12 α-helical transmembrane domain bracketed with cytoplasmically located N-and C-terminal hydrophilic regions . Transporters belonging to the AAAP family share minimal sequence homology and have an 11 α-helical transmembrane domain (Trip et al 2004). …”

mentioning

confidence: 99%

Cloning and characterization of Fpmtr1, an amino acid transporter gene of Fusarium proliferatum (Gibberella intermedia)

Jeney

Béki

Keszthelyi

et al. 2007

J. Basic Microbiol.

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Fpmtr1, an amino acid transporter gene from Fusarium proliferatum was strongly expressed during conidial germination and repressed in late stationary phase. To identify the specific function of this gene, DeltaFpmtr1 knock-out mutants were generated by gene replacement. Vegetative growth of the DeltaFpmtr1 mutants was normal both in liquid and on solid media, but conidial germination was delayed. The DeltaFpmtr1 mutants and the wild type were equally fertile when used as males in sexual crosses, however if the mutants were used as the female parent then the fertility of the cross decreased dramatically. Inactivation of Fpmtr1 abolished vegetative self-incompatibility in strain ITEM 2287 of F. proliferatum, but the DeltaFpmtr1 mutants were still vegetatively incompatible with the other strains of the fungus. Endophytic colonization capability of the mutants, assessed on maize seedlings also was adversely affected. These data suggest that Fpmtr1 is involved in multiple developmental processes related to both sexual and parasexual events in F. proliferatum. Furthermore, the fungus might have problems in adapting to a less than optimal environment if this otherwise dispensable transporter has been inactivated.

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PcMtr, an aromatic and neutral aliphatic amino acid permease of Penicillium chrysogenum

Cited by 9 publications

References 31 publications

A novel fungal family of oligopeptide transporters identified by functional metatranscriptomics of soil eukaryotes

A novel fungal family of oligopeptide transporters identified by functional metatranscriptomics of soil eukaryotes

AgtA, the Dicarboxylic Amino Acid Transporter of Aspergillus nidulans , Is Concertedly Down-Regulated by Exquisite Sensitivity to Nitrogen Metabolite Repression and Ammonium-Elicited Endocytosis

Cloning and characterization of Fpmtr1, an amino acid transporter gene of Fusarium proliferatum (Gibberella intermedia)

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