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Transport Proteins for Microbial Adaptations
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Transport Proteins for Microbial Adaptations

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Microbiology".

Deadline for manuscript submissions: closed (20 October 2020) | Viewed by 17183

Special Issue Editors

Prof. Dr. Stathis Frillingos

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Guest Editor
1. Laboratory of Biological Chemistry, Department of Medicine, University of Ioannina, Ioannina, Greece
2. Institute of Biosciences, University Research Center of Ioannina (URCI), Ioannina, Greece
Interests: transport proteins; nucleobase/nucleoside permeases; structure-function relationships; Cys-scanning analysis; evolution-specificity relationships; enterobacteria
Special Issues, Collections and Topics in MDPI journals
Dr. Maria Botou

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Guest Editor
Laboratory of Biological Chemistry, Department of Medicine, University of Ioannina, Ioannina, Greece
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Transmembrane transport has been essential to control ion gradients, osmolarity, influx and efflux of nutrient or toxic substances, right from the beginnings of cellular life on Earth. The microorganisms living today have evolved a wide spectrum of active transport systems that cost energetically to the cells but are often vital for reproductive success in various natural or symbiotic environments. Some of these systems, like the bacterial sugar-transporting phosphotransferase systems, multi-subunit ATP-binding cassette transporters, light-driven ion pumps, ion-translocating decarboxylases, thermophilic and extremophilic transport proteins, are unique or almost unique to prokaryotic microorganisms. Some are important for the exchange of metabolites in symbiotic consortia like the gut microbiome or the rhizosphere. Others are associated with endosymbiotic parasitism. The realm of transporter functions and specificities in the microbial transportomes is far from having been explored thoroughly to date. Also, the molecular underpinnings of different substrate specificities especially in secondary active transporters often remain elusive, due to the multitude of homologs and scarcity of structure-functional studies on many transporter families. In this Special Issue, we aim to collect original research or review articles discussing aspects of the evolution of transporter specificities associated with adaptations in bacteria, archaea, protists or fungi. We would like to dedicate this special issue to H. Ronald Kaback (1936-2019), whose seminal work on lac permease shaped the academic life of so many researchers in the field of active membrane transport.   

Prof. Dr. Stathis Frillingos
Dr. Maria Botou
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

  • evolution
  • membrane
  • transport
  • bacteria
  • microbiome
  • rhizosphere
  • archaea
  • protists
  • fungi
  • active transport
  • substrate specificity

Related Special Issue

Published Papers (5 papers)

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Research

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12 pages, 1894 KiB  
Article
Specificity of Interactions between Components of Two Zinc ABC Transporters in Paracoccus denitrificans
by Ady Berenice Meléndez, Daniel Valencia and Erik Thomas Yukl
Int. J. Mol. Sci. 2020, 21(23), 9098; https://doi.org/10.3390/ijms21239098 - 30 Nov 2020
Cited by 2 | Viewed by 2033
Abstract
Bacterial ATP binding cassette (ABC) transporters mediate the influx of numerous substrates. The cluster A-I ABC transporters are responsible for the specific uptake of the essential metals zinc, manganese or iron, making them necessary for survival in metal-limited environments, which for pathogens include [...] Read more.
Bacterial ATP binding cassette (ABC) transporters mediate the influx of numerous substrates. The cluster A-I ABC transporters are responsible for the specific uptake of the essential metals zinc, manganese or iron, making them necessary for survival in metal-limited environments, which for pathogens include the animal host. In Paracoccus denitrificans, there are two zinc ABC transporter systems: ZnuABC and AztABCD with apparently redundant functions under zinc-limited conditions. The unusual presence of two zinc ABC transporter systems in the same organism allowed for the investigation of specificity in the interaction between the solute binding protein (SBP) and its cognate permease. We also assessed the role of flexible loop features in the SBP in permease binding and zinc transport. The results indicate that the SBP–permease interaction is highly specific and does not require the flexible loop features of the SBP. We also present an expanded table of the properties of characterized cluster A-I SBPs and a multiple sequence alignment highlighting the conserved features. Through this analysis, an apparently new family of binding proteins associated with ABC transporters was identified. The presence of homologues in several human pathogens raises the possibility of using it as a target for the development of new antimicrobial therapies. Full article
(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations)
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17 pages, 2290 KiB  
Article
Function and Regulation of the Pyruvate Transporter CstA in Escherichia coli
by Ana Gasperotti, Stephanie Göing, Elena Fajardo-Ruiz, Ignasi Forné and Kirsten Jung
Int. J. Mol. Sci. 2020, 21(23), 9068; https://doi.org/10.3390/ijms21239068 - 28 Nov 2020
Cited by 13 | Viewed by 3742
Abstract
Pyruvate is a central metabolite that connects many metabolic pathways in living organisms. To meet the cellular pyruvate requirements, the enterobacterium Escherichia coli has at least three pyruvate uptake systems—the H+/pyruvate symporter BtsT, and two thus far less well-characterized transporters, YhjX [...] Read more.
Pyruvate is a central metabolite that connects many metabolic pathways in living organisms. To meet the cellular pyruvate requirements, the enterobacterium Escherichia coli has at least three pyruvate uptake systems—the H+/pyruvate symporter BtsT, and two thus far less well-characterized transporters, YhjX and CstA. BtsT and CstA belong to the putative carbon starvation (CstA) family (transporter classification TC# 2.A.114). We have created an E. coli mutant that cannot grow on pyruvate as the sole carbon source and used it to characterize CstA as a pyruvate transporter. Transport studies in intact cells confirmed that CstA is a highly specific pyruvate transporter with moderate affinity and is energized by a proton gradient. When cells of a reporter strain were cultured in complex medium, cstA expression was maximal only in stationary phase. A DNA affinity-capture assay combined with mass spectrometry and an in-vivo reporter assay identified Fis as a repressor of cstA expression, in addition to the known activator cAMP-CRP. The functional characterization and regulation of this second pyruvate uptake system provides valuable information for understanding the complexity of pyruvate sensing and uptake in E. coli. Full article
(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations)
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17 pages, 5373 KiB  
Article
A Single Cysteine Residue in the Translocation Pathway of the Mitosomal ADP/ATP Carrier from Cryptosporidium parvum Confers a Broad Nucleotide Specificity
by Martin S. King, Sotiria Tavoulari, Vasiliki Mavridou, Alannah C. King, John Mifsud and Edmund R. S. Kunji
Int. J. Mol. Sci. 2020, 21(23), 8971; https://doi.org/10.3390/ijms21238971 - 26 Nov 2020
Cited by 5 | Viewed by 2819
Abstract
Cryptosporidiumparvum is a clinically important eukaryotic parasite that causes the disease cryptosporidiosis, which manifests with gastroenteritis-like symptoms. The protist has mitosomes, which are organelles of mitochondrial origin that have only been partially characterized. The genome encodes a highly reduced set of transport [...] Read more.
Cryptosporidiumparvum is a clinically important eukaryotic parasite that causes the disease cryptosporidiosis, which manifests with gastroenteritis-like symptoms. The protist has mitosomes, which are organelles of mitochondrial origin that have only been partially characterized. The genome encodes a highly reduced set of transport proteins of the SLC25 mitochondrial carrier family of unknown function. Here, we have studied the transport properties of one member of the C. parvum carrier family, demonstrating that it resembles the mitochondrial ADP/ATP carrier of eukaryotes. However, this carrier has a broader substrate specificity for nucleotides, transporting adenosine, thymidine, and uridine di- and triphosphates in contrast to its mitochondrial orthologues, which have a strict substrate specificity for ADP and ATP. Inspection of the putative translocation pathway highlights a cysteine residue, which is a serine in mitochondrial ADP/ATP carriers. When the serine residue is replaced by cysteine or larger hydrophobic residues in the yeast mitochondrial ADP/ATP carrier, the substrate specificity becomes broad, showing that this residue is important for nucleotide base selectivity in ADP/ATP carriers. Full article
(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations)
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Review

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21 pages, 3076 KiB  
Review
Prokaryotic Solute/Sodium Symporters: Versatile Functions and Mechanisms of a Transporter Family
by Tania Henriquez, Larissa Wirtz, Dan Su and Heinrich Jung
Int. J. Mol. Sci. 2021, 22(4), 1880; https://doi.org/10.3390/ijms22041880 - 13 Feb 2021
Cited by 18 | Viewed by 4341
Abstract
The solute/sodium symporter family (SSS family; TC 2.A.21; SLC5) consists of integral membrane proteins that use an existing sodium gradient to drive the uphill transport of various solutes, such as sugars, amino acids, vitamins, or ions across the membrane. This large family has [...] Read more.
The solute/sodium symporter family (SSS family; TC 2.A.21; SLC5) consists of integral membrane proteins that use an existing sodium gradient to drive the uphill transport of various solutes, such as sugars, amino acids, vitamins, or ions across the membrane. This large family has representatives in all three kingdoms of life. The human sodium/iodide symporter (NIS) and the sodium/glucose transporter (SGLT1) are involved in diseases such as iodide transport defect or glucose-galactose malabsorption. Moreover, the bacterial sodium/proline symporter PutP and the sodium/sialic acid symporter SiaT play important roles in bacteria–host interactions. This review focuses on the physiological significance and structural and functional features of prokaryotic members of the SSS family. Special emphasis will be given to the roles and properties of proteins containing an SSS family domain fused to domains typically found in bacterial sensor kinases. Full article
(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations)
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14 pages, 1115 KiB  
Review
Life and Death of Fungal Transporters under the Challenge of Polarity
by Sofia Dimou and George Diallinas
Int. J. Mol. Sci. 2020, 21(15), 5376; https://doi.org/10.3390/ijms21155376 - 29 Jul 2020
Cited by 10 | Viewed by 3409
Abstract
Eukaryotic plasma membrane (PM) transporters face critical challenges that are not widely present in prokaryotes. The two most important issues are proper subcellular traffic and targeting to the PM, and regulated endocytosis in response to physiological, developmental, or stress signals. Sorting of transporters [...] Read more.
Eukaryotic plasma membrane (PM) transporters face critical challenges that are not widely present in prokaryotes. The two most important issues are proper subcellular traffic and targeting to the PM, and regulated endocytosis in response to physiological, developmental, or stress signals. Sorting of transporters from their site of synthesis, the endoplasmic reticulum (ER), to the PM has been long thought, but not formally shown, to occur via the conventional Golgi-dependent vesicular secretory pathway. Endocytosis of specific eukaryotic transporters has been studied more systematically and shown to involve ubiquitination, internalization, and sorting to early endosomes, followed by turnover in the multivesicular bodies (MVB)/lysosomes/vacuole system. In specific cases, internalized transporters have been shown to recycle back to the PM. However, the mechanisms of transporter forward trafficking and turnover have been overturned recently through systematic work in the model fungus Aspergillus nidulans. In this review, we present evidence that shows that transporter traffic to the PM takes place through Golgi bypass and transporter endocytosis operates via a mechanism that is distinct from that of recycling membrane cargoes essential for fungal growth. We discuss these findings in relation to adaptation to challenges imposed by cell polarity in fungi as well as in other eukaryotes and provide a rationale of why transporters and possibly other housekeeping membrane proteins ‘avoid’ routes of polar trafficking. Full article
(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations)
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