Eukaryotic transporters for hydroxyderivatives of benzoic acid

Abstract Several yeast species catabolize hydroxyderivatives of benzoic acid. However, the nature of carriers responsible for transport of these compounds across the plasma membrane is currently unknown. In this study, we analyzed a family of genes coding for permeases belonging to the major facilit...

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Autores principales:	Andrea Cillingová, Igor Zeman, Renáta Tóth, Martina Neboháčová, Ivana Dunčková, Mária Hölcová, Michaela Jakúbková, Gabriela Gérecová, Leszek P. Pryszcz, Ľubomír Tomáška, Toni Gabaldón, Attila Gácser, Jozef Nosek
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/362c6032bebf4015a7da5f08f01d4e58
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spelling	oai:doaj.org-article:362c6032bebf4015a7da5f08f01d4e582021-12-02T15:05:37ZEukaryotic transporters for hydroxyderivatives of benzoic acid10.1038/s41598-017-09408-62045-2322https://doaj.org/article/362c6032bebf4015a7da5f08f01d4e582017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-09408-6https://doaj.org/toc/2045-2322Abstract Several yeast species catabolize hydroxyderivatives of benzoic acid. However, the nature of carriers responsible for transport of these compounds across the plasma membrane is currently unknown. In this study, we analyzed a family of genes coding for permeases belonging to the major facilitator superfamily (MFS) in the pathogenic yeast Candida parapsilosis. Our results revealed that these transporters are functionally equivalent to bacterial aromatic acid: H+ symporters (AAHS) such as GenK, MhbT and PcaK. We demonstrate that the genes HBT1 and HBT2 encoding putative transporters are highly upregulated in C. parapsilosis cells assimilating hydroxybenzoate substrates and the corresponding proteins reside in the plasma membrane. Phenotypic analyses of knockout mutants and hydroxybenzoate uptake assays provide compelling evidence that the permeases Hbt1 and Hbt2 transport the substrates that are metabolized via the gentisate (3-hydroxybenzoate, gentisate) and 3-oxoadipate pathway (4-hydroxybenzoate, 2,4-dihydroxybenzoate and protocatechuate), respectively. Our data support the hypothesis that the carriers belong to the AAHS family of MFS transporters. Phylogenetic analyses revealed that the orthologs of Hbt permeases are widespread in the subphylum Pezizomycotina, but have a sparse distribution among Saccharomycotina lineages. Moreover, these analyses shed additional light on the evolution of biochemical pathways involved in the catabolic degradation of hydroxyaromatic compounds.Andrea CillingováIgor ZemanRenáta TóthMartina NeboháčováIvana DunčkováMária HölcováMichaela JakúbkováGabriela GérecováLeszek P. PryszczĽubomír TomáškaToni GabaldónAttila GácserJozef NosekNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Andrea Cillingová Igor Zeman Renáta Tóth Martina Neboháčová Ivana Dunčková Mária Hölcová Michaela Jakúbková Gabriela Gérecová Leszek P. Pryszcz Ľubomír Tomáška Toni Gabaldón Attila Gácser Jozef Nosek Eukaryotic transporters for hydroxyderivatives of benzoic acid
description	Abstract Several yeast species catabolize hydroxyderivatives of benzoic acid. However, the nature of carriers responsible for transport of these compounds across the plasma membrane is currently unknown. In this study, we analyzed a family of genes coding for permeases belonging to the major facilitator superfamily (MFS) in the pathogenic yeast Candida parapsilosis. Our results revealed that these transporters are functionally equivalent to bacterial aromatic acid: H+ symporters (AAHS) such as GenK, MhbT and PcaK. We demonstrate that the genes HBT1 and HBT2 encoding putative transporters are highly upregulated in C. parapsilosis cells assimilating hydroxybenzoate substrates and the corresponding proteins reside in the plasma membrane. Phenotypic analyses of knockout mutants and hydroxybenzoate uptake assays provide compelling evidence that the permeases Hbt1 and Hbt2 transport the substrates that are metabolized via the gentisate (3-hydroxybenzoate, gentisate) and 3-oxoadipate pathway (4-hydroxybenzoate, 2,4-dihydroxybenzoate and protocatechuate), respectively. Our data support the hypothesis that the carriers belong to the AAHS family of MFS transporters. Phylogenetic analyses revealed that the orthologs of Hbt permeases are widespread in the subphylum Pezizomycotina, but have a sparse distribution among Saccharomycotina lineages. Moreover, these analyses shed additional light on the evolution of biochemical pathways involved in the catabolic degradation of hydroxyaromatic compounds.
format	article
author	Andrea Cillingová Igor Zeman Renáta Tóth Martina Neboháčová Ivana Dunčková Mária Hölcová Michaela Jakúbková Gabriela Gérecová Leszek P. Pryszcz Ľubomír Tomáška Toni Gabaldón Attila Gácser Jozef Nosek
author_facet	Andrea Cillingová Igor Zeman Renáta Tóth Martina Neboháčová Ivana Dunčková Mária Hölcová Michaela Jakúbková Gabriela Gérecová Leszek P. Pryszcz Ľubomír Tomáška Toni Gabaldón Attila Gácser Jozef Nosek
author_sort	Andrea Cillingová
title	Eukaryotic transporters for hydroxyderivatives of benzoic acid
title_short	Eukaryotic transporters for hydroxyderivatives of benzoic acid
title_full	Eukaryotic transporters for hydroxyderivatives of benzoic acid
title_fullStr	Eukaryotic transporters for hydroxyderivatives of benzoic acid
title_full_unstemmed	Eukaryotic transporters for hydroxyderivatives of benzoic acid
title_sort	eukaryotic transporters for hydroxyderivatives of benzoic acid
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/362c6032bebf4015a7da5f08f01d4e58
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Eukaryotic transporters for hydroxyderivatives of benzoic acid

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