ArticleExtremophiles : life under extreme conditions2016
Expression and functional analysis of two NhaD type antiporters from the halotolerant and alkaliphilic Halomonas sp. Y2.
Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- TPGPred: A Mixed-Feature-Driven Approach for Identifying Thermophilic Proteins Based on GradientBoosting.International journal of molecular sciences · 2024Article
- The difference of intestinal microbiota composition between Lantang and Landrace newborn piglets.BMC veterinary research · 2023Article
- Mechanism of TonB-dependent transport system in Halomonas alkalicola CICC 11012s in response to alkaline stress.Extremophiles : life under extreme conditions · 2021Article
- Polar or Charged Residues Located in Four Highly Conserved Motifs Play a Vital Role in the Function or pH Response of a UPF0118 Family NaFrontiers in microbiology · 2020Article
- Characterization of a Functionally Unknown Arginine-Aspartate-Aspartate Family Protein FromFrontiers in microbiology · 2018Article
- Critical Functions of Region 1-67 and Helix XIII in Retaining the Active Structure of NhaD Antiporter inFrontiers in microbiology · 2018Article
- Functional Interaction between the N and C Termini of NhaD Antiporters from Halomonas sp. Strain Y2.Journal of bacteriology · 2017Article
- Characterization of a novel two-component NaScientific reports · 2017Article
- A UPF0118 family protein with uncharacterized function from the moderate halophile Halobacillus andaensis represents a novel class of NaScientific reports · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Na(+)/H(+) antiporters play important roles in ion and pH homeostasis. In this study, two NhaD homologues that effectively catalyze Na(+)/H(+) antiporter were identified from Halomonas sp. Y2, a halotolerant and alkaliphilic strain isolated from sodium enriched black liquor. They exhibited high sequence identity of 72 % and similar binding affinities for Na(+) and Li(+) translocation, while having different pH profiles. Ha-NhaD1 was active at pH 6.0 and most active at pH 8.0-8.5, whereas Ha-NhaD2 lacked activity at pH 6.0 but exhibited maximum activity at pH 9.5 or higher. Based on multiple alignments, 11 partially conserved residues were selected and corresponding mutants were generated for Ha-NhaD1. As expected, replacement of most of the hydrophobic residues abolished the cation exchange activities. Three serine residues at positions 200, 282 and 353 in Ha-NhaD1 were replaceable by alanines with partial retention of activity. The S353A mutant exhibited significantly reduced binding affinity for Na(+) and Li(+), while S282 mutant exhibited an alkaline shift of about 1.5 pH units, as compared to the wild type Ha-NhaD1. Serine at position 282 was predicted to be located in transmembrane segment VIII and was found to be important in regulating pH sensitivity in concert with flanking residues.
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