The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity

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...

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Main Authors: Wong, Chui-Fann, Grüber, Gerhard
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2021
Subjects:
Science::Biological sciences
Mycobacterium
Tuberculosis
Online Access:https://hdl.handle.net/10356/149232
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.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
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Science::Biological sciences
Mycobacterium
Tuberculosis
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
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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Wong, Chui-Fann
Grüber, Gerhard
format Article
author Wong, Chui-Fann
Grüber, Gerhard
author_sort Wong, Chui-Fann
title 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_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_sort unique c-terminal extension of mycobacterial f-atp synthase subunit α is the major contributor to its latent atp hydrolysis activity
publishDate 2021
url https://hdl.handle.net/10356/149232
_version_ 1759857019354873856

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