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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 (31 October 2021) | Viewed by 17094

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Prof. Dr. Stathis Frillingos

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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
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Dr. Maria Botou

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Laboratory of Biological Chemistry, Department of Medicine, University of Ioannina, Ioannina, Greece
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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

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Keywords

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

Related Special Issue

Transport Proteins for Microbial Adaptations in International Journal of Molecular Sciences (5 articles)

Published Papers (7 papers)

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Research

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18 pages, 1713 KiB

Open AccessArticle

New Insights on Heme Uptake in Leishmania spp.

by María Cabello-Donayre, Lina M. Orrego, Elisa Herráez, Raquel García-Hernández and José M. Pérez-Victoria

Int. J. Mol. Sci. 2022, 23(18), 10501; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms231810501 - 10 Sep 2022

Cited by 1 | Viewed by 1413

Abstract

The protozoan parasite Leishmania, responsible for leishmaniasis, is one of the few aerobic organisms that cannot synthesize the essential molecule heme. Therefore, it has developed specialized pathways to scavenge it from its host. In recent years, some proteins involved in the import of heme, such as LHR1 and LFLVCRB, have been identified, but relevant aspects regarding the process remain unknown. Here, we characterized the kinetics of the uptake of the heme analogue Zn(II) Mesoporphyrin IX (ZnMP) in Leishmania major promastigotes as a model of a parasite causing cutaneous leishmaniasis with special focus on the force that drives the process. We found that ZnMP uptake is an active, inducible, and pH-dependent process that does not require a plasma membrane proton gradient but requires the presence of the monovalent cations Na⁺ and/or K⁺. In addition, we demonstrated that this parasite can efflux this porphyrin against a concentration gradient. We also found that ZnMP uptake differs among different dermotropic or viscerotropic Leishmania species and does not correlate with LHR1 or LFLVCRB expression levels. Finally, we showed that these transporters have only partially overlapping functions. Altogether, these findings contribute to a deeper understanding of an important process in the biology of this parasite. Full article

(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations 2.0)

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17 pages, 3154 KiB

Open AccessArticle

Differences in Transporters Rather than Drug Targets Are the Principal Determinants of the Different Innate Sensitivities of Trypanosoma congolense and Trypanozoon Subgenus Trypanosomes to Diamidines and Melaminophenyl Arsenicals

by Marzuq A. Ungogo, Gustavo D. Campagnaro, Ali H. Alghamdi, Manal J. Natto and Harry P. de Koning

Int. J. Mol. Sci. 2022, 23(5), 2844; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23052844 - 05 Mar 2022

Cited by 9 | Viewed by 2066

Abstract

The animal trypanosomiases are infections in a wide range of (domesticated) animals with any species of African trypanosome, such as Trypanosoma brucei, T. evansi, T. congolense, T. equiperdum and T. vivax. Symptoms differ between host and infective species and stage of infection and are treated with a small set of decades-old trypanocides. A complication is that not all trypanosome species are equally sensitive to all drugs and the reasons are at best partially understood. Here, we investigate whether drug transporters, mostly identified in T. b. brucei, determine the different drug sensitivities. We report that homologues of the aminopurine transporter TbAT1 and the aquaporin TbAQP2 are absent in T. congolense, while their introduction greatly sensitises this species to diamidine (pentamidine, diminazene) and melaminophenyl (melarsomine) drugs. Accumulation of these drugs in the transgenic lines was much more rapid. T. congolense is also inherently less sensitive to suramin than T. brucei, despite accumulating it faster. Expression of a proposed suramin transporter, located in T. brucei lysosomes, in T. congolense, did not alter its suramin sensitivity. We conclude that for several of the most important classes of trypanocides the presence of specific transporters, rather than drug targets, is the determining factor of drug efficacy. Full article

(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations 2.0)

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12 pages, 1400 KiB

Open AccessArticle

Myristic Acid Inhibits the Activity of the Bacterial ABC Transporter BmrA

by Kristin Oepen, Hüseyin Özbek, Anja Schüffler, Johannes C. Liermann, Eckhard Thines and Dirk Schneider

Int. J. Mol. Sci. 2021, 22(24), 13565; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms222413565 - 17 Dec 2021

Cited by 6 | Viewed by 2599

Abstract

ATP-binding cassette (ABC) transporters are conserved in all kingdoms of life, where they transport substrates against a concentration gradient across membranes. Some ABC transporters are known to cause multidrug resistances in humans and are able to transport chemotherapeutics across cellular membranes. Similarly, BmrA, the ABC transporter of Bacillus subtilis, is involved in excretion of certain antibiotics out of bacterial cells. Screening of extract libraries isolated from fungi revealed that the C14 fatty acid myristic acid has an inhibitory effect on the BmrA ATPase as well as the transport activity. Thus, a natural membrane constituent inhibits the BmrA activity, a finding with physiological consequences as to the activity and regulation of ABC transporter activities in biological membranes. Full article

(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations 2.0)

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18 pages, 2699 KiB

Open AccessArticle

The Bul1/2 Alpha-Arrestins Promote Ubiquitylation and Endocytosis of the Can1 Permease upon Cycloheximide-Induced TORC1-Hyperactivation

by Amalia H. Megarioti, Cecilia Primo, George C. Kapetanakis, Alexandros Athanasopoulos, Vicky Sophianopoulou, Bruno André and Christos Gournas

Int. J. Mol. Sci. 2021, 22(19), 10208; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms221910208 - 22 Sep 2021

Cited by 4 | Viewed by 2160

Abstract

Selective endocytosis followed by degradation is a major mechanism for downregulating plasma membrane transporters in response to specific environmental cues. In Saccharomyces cerevisiae, this endocytosis is promoted by ubiquitylation catalyzed by the Rsp5 ubiquitin-ligase, targeted to transporters via adaptors of the alpha-arrestin family. However, the molecular mechanisms of this targeting and their control according to conditions remain incompletely understood. In this work, we dissect the molecular mechanisms eliciting the endocytosis of Can1, the arginine permease, in response to cycloheximide-induced TORC1 hyperactivation. We show that cycloheximide promotes Rsp5-dependent Can1 ubiquitylation and endocytosis in a manner dependent on the Bul1/2 alpha-arrestins. Also crucial for this downregulation is a short acidic patch sequence in the N-terminus of Can1 likely acting as a binding site for Bul1/2. The previously reported inhibition by cycloheximide of transporter recycling, from the trans-Golgi network to the plasma membrane, seems to additionally contribute to efficient Can1 downregulation. Our results also indicate that, contrary to the previously described substrate-transport elicited Can1 endocytosis mediated by the Art1 alpha-arrestin, Bul1/2-mediated Can1 ubiquitylation occurs independently of the conformation of the transporter. This study provides further insights into how distinct alpha-arrestins control the ubiquitin-dependent downregulation of a specific amino acid transporter under different conditions. Full article

(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations 2.0)

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14 pages, 4309 KiB

Open AccessArticle

Major Facilitator Superfamily Transporter Gene FgMFS1 Is Essential for Fusarium graminearum to Deal with Salicylic Acid Stress and for Its Pathogenicity towards Wheat

by Qing Chen, Lu Lei, Caihong Liu, Yazhou Zhang, Qiang Xu, Jing Zhu, Zhenru Guo, Yan Wang, Qingcheng Li, Yang Li, Li Kong, Yunfeng Jiang, Xiujin Lan, Jirui Wang, Qiantao Jiang, Guoyue Chen, Jian Ma, Yuming Wei, Youliang Zheng and Pengfei Qi

Int. J. Mol. Sci. 2021, 22(16), 8497; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22168497 - 07 Aug 2021

Cited by 4 | Viewed by 3237

Abstract

Wheat is a major staple food crop worldwide, due to its total yield and unique processing quality. Its grain yield and quality are threatened by Fusarium head blight (FHB), which is mainly caused by Fusarium graminearum. Salicylic acid (SA) has a strong and toxic effect on F. graminearum and is a hopeful target for sustainable control of FHB. F. graminearum is capable of efficientdealing with SA stress. However, the underlying mechanisms remain unclear. Here, we characterized FgMFS1 (FGSG_03725), a major facilitator superfamily (MFS) transporter gene in F. graminearum. FgMFS1 was highly expressed during infection and was upregulated by SA. The predicted three-dimensional structure of the FgMFS1 protein was consistent with the schematic for the antiporter. The subcellular localization experiment indicated that FgMFS1 was usually expressed in the vacuole of hyphae, but was alternatively distributed in the cell membrane under SA treatment, indicating an element of F. graminearum in response to SA. ΔFgMFS1 (loss of function mutant of FgMFS1) showed enhanced sensitivity to SA, less pathogenicity towards wheat, and reduced DON production under SA stress. Re-introduction of a functional FgMFS1 gene into ∆FgMFS1 recovered the mutant phenotypes. Wheat spikes inoculated with ΔFgMFS1 accumulated more SA when compared to those inoculated with the wild-type strain. Ecotopic expression of FgMFS1 in yeast enhanced its tolerance to SA as expected, further demonstrating that FgMFS1 functions as an SA exporter. In conclusion, FgMFS1 encodes an SA exporter in F. graminearum, which is critical for its response to wheat endogenous SA and pathogenicity towards wheat. Full article

(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations 2.0)

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17 pages, 3794 KiB

Open AccessArticle

Heterodimer Formation of the Homodimeric ABC Transporter OpuA

by Patricia Alvarez-Sieiro, Hendrik R. Sikkema and Bert Poolman

Int. J. Mol. Sci. 2021, 22(11), 5912; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22115912 - 31 May 2021

Cited by 3 | Viewed by 2535

Abstract

Many proteins have a multimeric structure and are composed of two or more identical subunits. While this can be advantageous for the host organism, it can be a challenge when targeting specific residues in biochemical analyses. In vitro splitting and re-dimerization to circumvent this problem is a tedious process that requires stable proteins. We present an in vivo approach to transform homodimeric proteins into apparent heterodimers, which then can be purified using two-step affinity-tag purification. This opens the door to both practical applications such as smFRET to probe the conformational dynamics of homooligomeric proteins and fundamental research into the mechanism of protein multimerization, which is largely unexplored for membrane proteins. We show that expression conditions are key for the formation of heterodimers and that the order of the differential purification and reconstitution of the protein into nanodiscs is important for a functional ABC-transporter complex. Full article

(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations 2.0)

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Review

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10 pages, 2611 KiB

Open AccessReview

Function Trumps Form in Two Sugar Symporters, LacY and vSGLT

by Jeff Abramson and Ernest M. Wright

Int. J. Mol. Sci. 2021, 22(7), 3572; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22073572 - 30 Mar 2021

Cited by 5 | Viewed by 2302

Abstract

Active transport of sugars into bacteria occurs through symporters driven by ion gradients. LacY is the most well-studied proton sugar symporter, whereas vSGLT is the most characterized sodium sugar symporter. These are members of the major facilitator (MFS) and the amino acid-Polyamine organocation (APS) transporter superfamilies. While there is no structural homology between these transporters, they operate by a similar mechanism. They are nano-machines driven by their respective ion electrochemical potential gradients across the membrane. LacY has 12 transmembrane helices (TMs) organized in two 6-TM bundles, each containing two 3-helix TM repeats. vSGLT has a core structure of 10 TM helices organized in two inverted repeats (TM 1–5 and TM 6–10). In each case, a single sugar is bound in a central cavity and sugar selectivity is determined by hydrogen- and hydrophobic- bonding with side chains in the binding site. In vSGLT, the sodium-binding site is formed through coordination with carbonyl- and hydroxyl-oxygens from neighboring side chains, whereas in LacY the proton (H₃O⁺) site is thought to be a single glutamate residue (Glu325). The remaining challenge for both transporters is to determine how ion electrochemical potential gradients drive uphill sugar transport. Full article

(This article belongs to the Special Issue Transport Proteins for Microbial Adaptations 2.0)

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