The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity
Mycobacterial F1Fo-ATP synthases (α3:β3:γ:δ:ε:a:b:b':c9 ) are incapable of ATP-driven proton translocation due to their latent ATPase activity. This prevents wasting of ATP and altering of the proton motive force, whose dissipation is lethal to mycobacteria. We demonstrate that the mycobacteria...
| Main Authors: | , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
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2021
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| Online Access: | https://hdl.handle.net/10356/149232 |
| _version_ | 1811694829939195904 |
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| author | Wong, Chui-Fann Grüber, Gerhard |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Wong, Chui-Fann Grüber, Gerhard |
| author_sort | Wong, Chui-Fann |
| collection | NTU |
| description | Mycobacterial F1Fo-ATP synthases (α3:β3:γ:δ:ε:a:b:b':c9 ) are incapable of ATP-driven proton translocation due to their latent ATPase activity. This prevents wasting of ATP and altering of the proton motive force, whose dissipation is lethal to mycobacteria. We demonstrate that the mycobacterial C-terminal extension of nucleotide-binding subunit α contributes mainly to the suppression of ATPase activity in the recombinant mycobacterial F1-ATPase. Using C-terminal deletion mutants, the regions responsible for the enzyme's latency were mapped, providing a new compound epitope. |
| first_indexed | 2024-10-01T07:13:48Z |
| format | Journal Article |
| id | ntu-10356/149232 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:13:48Z |
| publishDate | 2021 |
| record_format | dspace |
| spelling | ntu-10356/1492322023-02-28T17:09:45Z The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity Wong, Chui-Fann Grüber, Gerhard School of Biological Sciences Science::Biological sciences Mycobacterium Tuberculosis Mycobacterial F1Fo-ATP synthases (α3:β3:γ:δ:ε:a:b:b':c9 ) are incapable of ATP-driven proton translocation due to their latent ATPase activity. This prevents wasting of ATP and altering of the proton motive force, whose dissipation is lethal to mycobacteria. We demonstrate that the mycobacterial C-terminal extension of nucleotide-binding subunit α contributes mainly to the suppression of ATPase activity in the recombinant mycobacterial F1-ATPase. Using C-terminal deletion mutants, the regions responsible for the enzyme's latency were mapped, providing a new compound epitope. National Research Foundation (NRF) Published version This work and the research scholarship of C.F.W. were supported by the National Research Foundation (NRF) Singapore, NRF Competitive Research Program (CRP) (grant NRF–CRP18–2017–01). 2021-05-18T07:10:04Z 2021-05-18T07:10:04Z 2020 Journal Article Wong, C. & Grüber, G. (2020). The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity. Antimicrobial Agents and Chemotherapy, 64(12). https://dx.doi.org/10.1128/AAC.01568-20 0066-4804 https://hdl.handle.net/10356/149232 10.1128/AAC.01568-20 32988828 2-s2.0-85096365257 12 64 en NRF–CRP18–2017–01 Antimicrobial Agents and Chemotherapy © 2020 American Society for Microbiology (ASM). All rights reserved. This paper was published in Antimicrobial Agents and Chemotherapy and is made available with permission of American Society for Microbiology (ASM). application/pdf |
| spellingShingle | Science::Biological sciences Mycobacterium Tuberculosis Wong, Chui-Fann Grüber, Gerhard The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity |
| title | The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity |
| title_full | The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity |
| title_fullStr | The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity |
| title_full_unstemmed | The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity |
| title_short | The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity |
| title_sort | unique c terminal extension of mycobacterial f atp synthase subunit α is the major contributor to its latent atp hydrolysis activity |
| topic | Science::Biological sciences Mycobacterium Tuberculosis |
| url | https://hdl.handle.net/10356/149232 |
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