@ARTICLE{TreeBASE2Ref28535,
author = {Rahul Salunke and Tobias Mourier and Manidipa Banerjee and Arnab Pain and Dhanasekaran Shanmuga},
title = {Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii},
year = {2018},
keywords = {},
doi = {},
url = {http://},
pmid = {},
journal = {PLoS Biology},
volume = {},
number = {},
pages = {},
abstract = {The mitochondrial F-type ATP synthase, a multi-subunit nanomotor, is critical for maintaining cellular ATP levels. In Toxoplasma gondii and other apicomplexan parasites, many subunit components, necessary for proper assembly and functioning of this enzyme, appear to be missing. Here, we report the identification of 20 novel subunits of T. gondii F-type ATP synthase from mass spectrometry analysis of partially purified monomer (~600 kDa) and dimer (>1 MDa) forms of the enzyme. Despite extreme sequence diversification, key FO subunits, a, b and d, can be identified from conserved structural features. Orthologs for many of these proteins are restricted to apicomplexan, chromerid and dinoflagellate species. Interestingly, their absence in ciliates indicates a major diversion, with respect to subunit composition of this enzyme, within the alveolate clade. Discovery of these highly diversified novel components of the apicomplexan F-type ATP synthase complex will facilitate the development of novel anti-parasitic agents. Structural and functional characterization of this unusual enzyme complex will advance our fundamental of energy metabolism in apicomplexan species}
}
Citation for Study 22877
Citation title:
"Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii".
Study name:
"Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii".
This study is part of submission 22877
(Status: Published).
Citation
Salunke R., Mourier T., Banerjee M., Pain A., & Shanmuga D. 2018. Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii. PLoS Biology, .
Authors
-
Salunke R.
-
Mourier T.
(submitter)
+45 60608342
-
Banerjee M.
-
Pain A.
-
Shanmuga D.
Abstract
The mitochondrial F-type ATP synthase, a multi-subunit nanomotor, is critical for maintaining cellular ATP levels. In Toxoplasma gondii and other apicomplexan parasites, many subunit components, necessary for proper assembly and functioning of this enzyme, appear to be missing. Here, we report the identification of 20 novel subunits of T. gondii F-type ATP synthase from mass spectrometry analysis of partially purified monomer (~600 kDa) and dimer (>1 MDa) forms of the enzyme. Despite extreme sequence diversification, key FO subunits, a, b and d, can be identified from conserved structural features. Orthologs for many of these proteins are restricted to apicomplexan, chromerid and dinoflagellate species. Interestingly, their absence in ciliates indicates a major diversion, with respect to subunit composition of this enzyme, within the alveolate clade. Discovery of these highly diversified novel components of the apicomplexan F-type ATP synthase complex will facilitate the development of novel anti-parasitic agents. Structural and functional characterization of this unusual enzyme complex will advance our fundamental of energy metabolism in apicomplexan species
External links
About this resource
- Canonical resource URI:
http://purl.org/phylo/treebase/phylows/study/TB2:S22877
- Other versions:
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NeXML
- Show BibTeX reference
@ARTICLE{TreeBASE2Ref28535,
author = {Rahul Salunke and Tobias Mourier and Manidipa Banerjee and Arnab Pain and Dhanasekaran Shanmuga},
title = {Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii},
year = {2018},
keywords = {},
doi = {},
url = {http://},
pmid = {},
journal = {PLoS Biology},
volume = {},
number = {},
pages = {},
abstract = {The mitochondrial F-type ATP synthase, a multi-subunit nanomotor, is critical for maintaining cellular ATP levels. In Toxoplasma gondii and other apicomplexan parasites, many subunit components, necessary for proper assembly and functioning of this enzyme, appear to be missing. Here, we report the identification of 20 novel subunits of T. gondii F-type ATP synthase from mass spectrometry analysis of partially purified monomer (~600 kDa) and dimer (>1 MDa) forms of the enzyme. Despite extreme sequence diversification, key FO subunits, a, b and d, can be identified from conserved structural features. Orthologs for many of these proteins are restricted to apicomplexan, chromerid and dinoflagellate species. Interestingly, their absence in ciliates indicates a major diversion, with respect to subunit composition of this enzyme, within the alveolate clade. Discovery of these highly diversified novel components of the apicomplexan F-type ATP synthase complex will facilitate the development of novel anti-parasitic agents. Structural and functional characterization of this unusual enzyme complex will advance our fundamental of energy metabolism in apicomplexan species}
}
- Show RIS reference
TY - JOUR
ID - 28535
AU - Salunke,Rahul
AU - Mourier,Tobias
AU - Banerjee,Manidipa
AU - Pain,Arnab
AU - Shanmuga,Dhanasekaran
T1 - Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii
PY - 2018
KW -
UR - http://dx.doi.org/
N2 - The mitochondrial F-type ATP synthase, a multi-subunit nanomotor, is critical for maintaining cellular ATP levels. In Toxoplasma gondii and other apicomplexan parasites, many subunit components, necessary for proper assembly and functioning of this enzyme, appear to be missing. Here, we report the identification of 20 novel subunits of T. gondii F-type ATP synthase from mass spectrometry analysis of partially purified monomer (~600 kDa) and dimer (>1 MDa) forms of the enzyme. Despite extreme sequence diversification, key FO subunits, a, b and d, can be identified from conserved structural features. Orthologs for many of these proteins are restricted to apicomplexan, chromerid and dinoflagellate species. Interestingly, their absence in ciliates indicates a major diversion, with respect to subunit composition of this enzyme, within the alveolate clade. Discovery of these highly diversified novel components of the apicomplexan F-type ATP synthase complex will facilitate the development of novel anti-parasitic agents. Structural and functional characterization of this unusual enzyme complex will advance our fundamental of energy metabolism in apicomplexan species
L3 -
JF - PLoS Biology
VL -
IS -
ER -
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