Functional Interaction between the N and C Termini of NhaD Antiporters from Halomonas sp. Strain Y2
Two NhaD-type antiporters, NhaD1 and NhaD2, from the halotolerant and alkaliphilic Halomonas sp. strain Y2, exhibit different physiological functions in regard to Na+ and Li+ resistance, although they share high sequence identity. In the present study, the truncation of an additional 4 C-terminal residues from NhaD2 or an exchange of 39 N-terminal residues between these proteins resulted in the complete loss of antiporter activity. Interestingly, combining 39 N-terminal residues and 7 C-terminal residues of NhaD2 (N39D2-C7) partially recovered the activity for Na+ and Li+ expulsion, as well as complementary growth following exposure to 300 mM Na+ and 100 mM Li+ stress. The recovered activity of chimera N39D2-C7 indicated that the N and C termini are structurally dependent on each other and function synergistically. Furthermore, fluorescence resonance energy transfer (FRET) analysis suggested that the N and C termini are relatively close in proximity which may account for their synergistic function in ion translocation. In the N-terminal region of N39D2-C7, the replacement of Glu38 with Pro abolished the recovered complementary and transport activities. In addition, this amino acid substitution in NhaD2 resulted in a drastically decreased complementation ability in Escherichia coli KNabc (level identical to that of NhaD1), as well as decreased activity and an altered pH profile..
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
2017 |
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| Erschienen: |
2017 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:199 |
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| Enthalten in: |
Journal of bacteriology - 199(2017), 16 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Yiwei Meng [VerfasserIn] |
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| Links: |
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| Förderinstitution / Projekttitel: |
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OLC199744254X |
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| 245 | 1 | 0 | |a Functional Interaction between the N and C Termini of NhaD Antiporters from Halomonas sp. Strain Y2 |
| 264 | 1 | |c 2017 | |
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| 520 | |a Two NhaD-type antiporters, NhaD1 and NhaD2, from the halotolerant and alkaliphilic Halomonas sp. strain Y2, exhibit different physiological functions in regard to Na+ and Li+ resistance, although they share high sequence identity. In the present study, the truncation of an additional 4 C-terminal residues from NhaD2 or an exchange of 39 N-terminal residues between these proteins resulted in the complete loss of antiporter activity. Interestingly, combining 39 N-terminal residues and 7 C-terminal residues of NhaD2 (N39D2-C7) partially recovered the activity for Na+ and Li+ expulsion, as well as complementary growth following exposure to 300 mM Na+ and 100 mM Li+ stress. The recovered activity of chimera N39D2-C7 indicated that the N and C termini are structurally dependent on each other and function synergistically. Furthermore, fluorescence resonance energy transfer (FRET) analysis suggested that the N and C termini are relatively close in proximity which may account for their synergistic function in ion translocation. In the N-terminal region of N39D2-C7, the replacement of Glu38 with Pro abolished the recovered complementary and transport activities. In addition, this amino acid substitution in NhaD2 resulted in a drastically decreased complementation ability in Escherichia coli KNabc (level identical to that of NhaD1), as well as decreased activity and an altered pH profile. | ||
| 540 | |a Nutzungsrecht: © COPYRIGHT 2017 American Society for Microbiology | ||
| 650 | 4 | |a Research | |
| 650 | 4 | |a Membrane proteins | |
| 650 | 4 | |a Halomonas | |
| 650 | 4 | |a Genetic aspects | |
| 650 | 4 | |a Fluorescence resonance energy transfer | |
| 650 | 4 | |a Fluorescence | |
| 650 | 4 | |a Amino acid substitution | |
| 650 | 4 | |a Residues | |
| 650 | 4 | |a Salinity tolerance | |
| 650 | 4 | |a Strain | |
| 650 | 4 | |a Bacterial infections | |
| 650 | 4 | |a Energy transfer | |
| 650 | 4 | |a Escherichia coli | |
| 650 | 4 | |a Proteins | |
| 650 | 4 | |a E coli | |
| 650 | 4 | |a pH effects | |
| 650 | 4 | |a Translocation | |
| 650 | 4 | |a Bacteriology | |
| 700 | 0 | |a Zhou Yang |4 oth | |
| 700 | 0 | |a Bin Cheng |4 oth | |
| 700 | 0 | |a Xinyu Nie |4 oth | |
| 700 | 0 | |a Shannan Li |4 oth | |
| 700 | 0 | |a Huijia Yin |4 oth | |
| 700 | 0 | |a Ping Xu |4 oth | |
| 700 | 0 | |a Chunyu Yang |4 oth | |
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