The C-H peripheral stalk base: a novel component in V1-ATPase assembly.
Vacuolar ATPases (V-ATPases) are molecular machines responsible for creating electrochemical gradients and preserving pH-dependent cellular compartments by way of proton translocation across the membrane. V-ATPases employ a dynamic rotary mechanism that is driven by ATP hydrolysis and the central ro...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2010-09-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2933246?pdf=render |
| _version_ | 1818938114862743552 |
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| author | Zacariah L Hildenbrand Sudheer K Molugu Daniela Stock Ricardo A Bernal |
| author_facet | Zacariah L Hildenbrand Sudheer K Molugu Daniela Stock Ricardo A Bernal |
| author_sort | Zacariah L Hildenbrand |
| collection | DOAJ |
| description | Vacuolar ATPases (V-ATPases) are molecular machines responsible for creating electrochemical gradients and preserving pH-dependent cellular compartments by way of proton translocation across the membrane. V-ATPases employ a dynamic rotary mechanism that is driven by ATP hydrolysis and the central rotor stalk. Regulation of this rotational catalysis is the result of a reversible V(1)V(o)-domain dissociation that is required to preserve ATP during instances of cellular starvation. Recently the method by which the free V(1)-ATPase abrogates the hydrolytic breakdown of ATP upon dissociating from the membrane has become increasingly clear. In this instance the central stalk subunit F adopts an extended conformation to engage in a bridging interaction tethering the rotor and stator components together. However, the architecture by which this mechanism is stabilized has remained ambiguous despite previous work. In an effort to elucidate the method by which the rotational catalysis is maintained, the architecture of the peripheral stalks and their respective binding interactions was investigated using cryo-electron microscopy. In addition to confirming the bridging interaction exuded by subunit F for the first time in a eukaryotic V-ATPase, subunits C and H are seen interacting with one another in a tight interaction that provides a base for the three EG peripheral stalks. The formation of a CE(3)G(3)H sub-assembly appears to be unique to the dissociated V-ATPase and highlights the stator architecture in addition to revealing a possible intermediate in the assembly mechanism of the free V(1)-ATPase. |
| first_indexed | 2024-12-20T06:02:43Z |
| format | Article |
| id | doaj.art-6200cf0c3f6444d4bb349d8f1c125bdc |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-20T06:02:43Z |
| publishDate | 2010-09-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-6200cf0c3f6444d4bb349d8f1c125bdc2022-12-21T19:50:52ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-09-0159e1258810.1371/journal.pone.0012588The C-H peripheral stalk base: a novel component in V1-ATPase assembly.Zacariah L HildenbrandSudheer K MoluguDaniela StockRicardo A BernalVacuolar ATPases (V-ATPases) are molecular machines responsible for creating electrochemical gradients and preserving pH-dependent cellular compartments by way of proton translocation across the membrane. V-ATPases employ a dynamic rotary mechanism that is driven by ATP hydrolysis and the central rotor stalk. Regulation of this rotational catalysis is the result of a reversible V(1)V(o)-domain dissociation that is required to preserve ATP during instances of cellular starvation. Recently the method by which the free V(1)-ATPase abrogates the hydrolytic breakdown of ATP upon dissociating from the membrane has become increasingly clear. In this instance the central stalk subunit F adopts an extended conformation to engage in a bridging interaction tethering the rotor and stator components together. However, the architecture by which this mechanism is stabilized has remained ambiguous despite previous work. In an effort to elucidate the method by which the rotational catalysis is maintained, the architecture of the peripheral stalks and their respective binding interactions was investigated using cryo-electron microscopy. In addition to confirming the bridging interaction exuded by subunit F for the first time in a eukaryotic V-ATPase, subunits C and H are seen interacting with one another in a tight interaction that provides a base for the three EG peripheral stalks. The formation of a CE(3)G(3)H sub-assembly appears to be unique to the dissociated V-ATPase and highlights the stator architecture in addition to revealing a possible intermediate in the assembly mechanism of the free V(1)-ATPase.http://europepmc.org/articles/PMC2933246?pdf=render |
| spellingShingle | Zacariah L Hildenbrand Sudheer K Molugu Daniela Stock Ricardo A Bernal The C-H peripheral stalk base: a novel component in V1-ATPase assembly. PLoS ONE |
| title | The C-H peripheral stalk base: a novel component in V1-ATPase assembly. |
| title_full | The C-H peripheral stalk base: a novel component in V1-ATPase assembly. |
| title_fullStr | The C-H peripheral stalk base: a novel component in V1-ATPase assembly. |
| title_full_unstemmed | The C-H peripheral stalk base: a novel component in V1-ATPase assembly. |
| title_short | The C-H peripheral stalk base: a novel component in V1-ATPase assembly. |
| title_sort | c h peripheral stalk base a novel component in v1 atpase assembly |
| url | http://europepmc.org/articles/PMC2933246?pdf=render |
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