Designating ligand specificities to metal uptake ABC transporters in <i>Thermus thermophilus</i> HB8

Mandal, Suraj Kumar; Adhikari, Rahi; Sharma, Anjaney; Chandravanshi, Monika; Gogoi, Prerana; Kanaujia, Shankar Prasad

doi:10.1039/c8mt00374b

Cited by 17 publications

(8 citation statements)

References 68 publications

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“…Heavy metal transport proteins play a key role in microbiological metabolism under Cd stress. In particular, ATP binding cassette transporters (ABC transporters) responsible for maintaining metal ion homeostasis by transporting metal ions across the cell membrane, either as naked ions or in the form of various complexes [20,21]. In this work, 7 ABC transporters were identified in M. spongiola; their mean change in expression was 1.006< log 2 FC <15.776 (Table S6).…”

Section: Expression Of Transporter Proteins In M Spongiola Under Cd Stressmentioning

confidence: 82%

“…In this study, a large number of transporter genes were remarkably induced in different Cd-treatment groups, including 7 ATP binding cassette transporter (ABC transporter), 3 Multidrug resistance protein (MRP), 4 Copper transporter (CTR), 4 Zinc transporter (ZRT), 3 Heavy metal transporter (HMT), 1 Cation transport ATPase (CE) and 1 Iron transport multicopper (ILT) (Table S6). ABC transporters, as one of the largest families of microbial membrane proteins, shows great important in resisting virulence and drug, especially in the function of maintaining metal ion homeostasis by transporting metal ions across the cell membrane in ionic/complex forms [20,21]. It was reported that the expression of 3 ABC genes (EpABC2.1, EpABC3.1, or EpABC4.1) of dominant dark septate endophytes (DSEs) could promote the restoring growth of metal-sensitive mutant by alleviating the inhibitory activity in yeast caused by Pb, Zn and Cd, and further altered toxic ions uptake and accumulation [27].…”

Section: Mechanisms Of CD Stress Resistance In M Spongiolamentioning

confidence: 99%

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Transcriptome Analysis and Expression Profiling of Molecular Responses to Cd Toxicity in Morchella spongiola

Xie

Jiang

et al. 2021

Mycobiology

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Morchella is a genus of fungi with the ability to concentrate Cd both in the fruit-body and mycelium. However, the molecular mechanisms conferring resistance to Cd stress in Morchella are unknown. Here, RNA-based transcriptomic sequencing was used to identify the genes and pathways involved in Cd tolerance in Morchella spongiola. 7444 differentially expressed genes (DEGs) were identified by cultivating M. spongiola in media containing 0.15, 0.90, or 1.50 mg/L Cd 2þ . The DEGs were divided into six sub-clusters based on their global expression profiles. GO enrichment analysis indicated that numerous DEGs were associated with catalytic activity, cell cycle control, and the ribosome. KEGG enrichment analysis showed that the main pathways under Cd stress were MAPK signaling, oxidative phosphorylation, pyruvate metabolism, and propanoate metabolism. In addition, several DEGs encoding ion transporters, enzymatic/non-enzymatic antioxidants, and transcription factors were identified. Based on these results, a preliminary gene regulatory network was firstly proposed to illustrate the molecular mechanisms of Cd detoxification in M. spongiola. These results provide valuable insights into the Cd tolerance mechanism of M. spongiola and constitute a robust foundation for further studies on detoxification mechanisms in macrofungi that could potentially lead to the development of new and improved fungal bioremediation strategies.

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Section: Expression Of Transporter Proteins In M Spongiola Under Cd Stressmentioning

confidence: 82%

Section: Mechanisms Of CD Stress Resistance In M Spongiolamentioning

confidence: 99%

Transcriptome Analysis and Expression Profiling of Molecular Responses to Cd Toxicity in Morchella spongiola

Xie

Jiang

et al. 2021

Mycobiology

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“…Thermophilic microorganisms are capable of surviving in diverse habitats such as geothermal springs, volcanic areas, hot water regions, marine hydrothermal vents and geothermal power plants (Ranawat & Rawat, 2018). Such punitive environments rich in metal, metalloid and metal-ion complexes necessitate the availability of specific metal-uptake transporters in the microorganisms (Mandal et al, 2019). Among the various functions of divalent metal ions in cellular and physiological processes, one of the important functions is to stimulate the uptake of citrate molecules in prokaryotes (Krom et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…Thermus thermophilus is one such well studied Gram-negative thermophilic bacterium that resides in marine hot springs and can grow at temperatures of $50-82 C (Alarico et al, 2005;Ohtani et al, 2012). Previously, using an in silico analysis we have reported the presence of an Mg 2+ /Fe 3+ -complexed citrate-transport system in T. thermophilus HB8 (Mandal et al, 2019). In this study, we confirm the presence of a divalent metal ion-stimulated citrate-binding protein (ORF TTHB177; hereafter referred to as metal ion citrate transporter A, MctA).…”

Section: Introductionmentioning

confidence: 99%

Structural and thermodynamic insights into a novel Mg²⁺–citrate-binding protein from the ABC transporter superfamily

Mandal¹,

Kanaujia²

2021

Acta Crystallogr D Struct Biol

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More than one third of proteins require metal ions to accomplish their functions, making them obligatory for the growth and survival of microorganisms in varying environmental niches. In prokaryotes, besides their involvement in various cellular and physiological processes, metal ions stimulate the uptake of citrate molecules. Citrate is a source of carbon and energy and is reported to be transported by secondary transporters. In Gram-positive bacteria, citrate molecules are transported in complex with divalent metal ions, whereas in Gram-negative bacteria they are translocated by Na+/citrate symporters. In this study, the presence of a novel divalent-metal-ion-complexed citrate-uptake system that belongs to the primary active ABC transporter superfamily is reported. For uptake, the metal-ion-complexed citrate molecules are sequestered by substrate-binding proteins (SBPs) and transferred to transmembrane domains for their transport. This study reports crystal structures of an Mg2+–citrate-binding protein (MctA) from the Gram-negative thermophilic bacterium Thermus thermophilus HB8 in both apo and holo forms in the resolution range 1.63–2.50 Å. Despite binding various divalent metal ions, MctA possesses the coordination geometry to bind its physiological metal ion, Mg2+. The results also suggest an extended subclassification of cluster D SBPs, which are known to bind and transport divalent-metal-ion-complexed citrate molecules. Comparative assessment of the open and closed conformations of the wild-type and mutant MctA proteins suggests a gating mechanism of ligand entry following an `asymmetric domain movement' of the N-terminal domain for substrate binding.

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mentioning

confidence: 99%

Understanding the structural and functional aspects of a novel Mg²⁺ citrate-binding protein

Mandal¹,

Kanaujia²

2021

Acta Cryst Sect A

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Nearly one-third of the proteins require metal ions to accomplish their functions, making them obligatory for the growth and survival of microorganisms in varying environmental niches [1,2]. In prokaryotes, besides their involvement in various cellular and physiological processes, metal ions stimulate the uptake of citrate molecules. Citrate is a source of carbon and energy and is reported to be transported by secondary transporters. In Gram-positive bacteria, citrate molecules are transported in complex with divalent metal ions, whereas in Gramnegative bacteria, they are translocated by Na + /citrate symporters (CitS) [3,4]. Interestingly, the presence of a secondary transporter allowing the translocation of divalent metal ion-complexed citrate in Gram-negative bacteria has not been reported till date. In this study, we report the presence of a novel divalent metal ion-complexed citrate uptake system that belongs to the primary active ABC transporter superfamily. For the uptake, the metal ion-complexed citrate molecules are sequestered by substrate-binding proteins (SBPs) and transferred to transmembrane domains (TMDs) for their transport [1,2]. Since SBPs are involved in maintaining the selectivity and specificity of the substrate(s) and directionality of the transport, they have been reported to be pivotal. This study reports the crystal structures of an Mg 2+ -citrate-binding protein (MctA) from a Gram-negative thermophilic bacteria Thermus thermophilus HB8 in both apo and holo forms at a resolution range of 1.63 to 2.50 Å. Despite binding various divalent metal ions, MctA follows the coordination geometry to bind its physiological metal ion, Mg 2+ . The results also suggest a novel subclassification of cluster D SBPs, known to bind and transport divalent metal ion-complexed citrate molecules. Comparative assessment of the open and closed conformations of the wild-type and mutant proteins of MctA suggests a gating mechanism of ligand entry following an "asymmetric domain movement" of the N-terminal domain (NTD) for substrate binding.Figure 1. The protein MctA recognizes and binds Mg 2+ -citrate in the periplasm and transfer it to the MctBC transport system for further translocation of the substrate.

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Designating ligand specificities to metal uptake ABC transporters in Thermus thermophilus HB8

Abstract: Acquisition of different metal ions by metal uptake ABC transporters of Thermus thermophilus HB8 for accomplishing its various cellular functions.

Cited by 17 publications

References 68 publications

Transcriptome Analysis and Expression Profiling of Molecular Responses to Cd Toxicity in Morchella spongiola

Transcriptome Analysis and Expression Profiling of Molecular Responses to Cd Toxicity in Morchella spongiola

Structural and thermodynamic insights into a novel Mg²⁺–citrate-binding protein from the ABC transporter superfamily

Understanding the structural and functional aspects of a novel Mg²⁺ citrate-binding protein

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Designating ligand specificities to metal uptake ABC transporters in Thermus thermophilus HB8

Abstract: Acquisition of different metal ions by metal uptake ABC transporters of Thermus thermophilus HB8 for accomplishing its various cellular functions.

Cited by 17 publications

References 68 publications

Transcriptome Analysis and Expression Profiling of Molecular Responses to Cd Toxicity in Morchella spongiola

Transcriptome Analysis and Expression Profiling of Molecular Responses to Cd Toxicity in Morchella spongiola

Structural and thermodynamic insights into a novel Mg2+–citrate-binding protein from the ABC transporter superfamily

Understanding the structural and functional aspects of a novel Mg2+ citrate-binding protein

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Product

Resources

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Structural and thermodynamic insights into a novel Mg²⁺–citrate-binding protein from the ABC transporter superfamily

Understanding the structural and functional aspects of a novel Mg²⁺ citrate-binding protein