Cargando…
The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli
MoxR ATPases are widespread throughout bacteria and archaea. The experimental evidence to date suggests that these proteins have chaperone-like roles in facilitating the maturation of dedicated protein complexes that are functionally diverse. In Escherichia coli, the MoxR ATPase RavA and its putativ...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3893208/ https://www.ncbi.nlm.nih.gov/pubmed/24454883 http://dx.doi.org/10.1371/journal.pone.0085529 |
_version_ | 1782299642248036352 |
---|---|
author | Wong, Keith S. Snider, Jamie D. Graham, Chris Greenblatt, Jack F. Emili, Andrew Babu, Mohan Houry, Walid A. |
author_facet | Wong, Keith S. Snider, Jamie D. Graham, Chris Greenblatt, Jack F. Emili, Andrew Babu, Mohan Houry, Walid A. |
author_sort | Wong, Keith S. |
collection | PubMed |
description | MoxR ATPases are widespread throughout bacteria and archaea. The experimental evidence to date suggests that these proteins have chaperone-like roles in facilitating the maturation of dedicated protein complexes that are functionally diverse. In Escherichia coli, the MoxR ATPase RavA and its putative cofactor ViaA are found to exist in early stationary-phase cells at 37°C at low levels of about 350 and 90 molecules per cell, respectively. Both proteins are predominantly localized to the cytoplasm, but ViaA was also unexpectedly found to localize to the cell membrane. Whole genome microarrays and synthetic lethality studies both indicated that RavA-ViaA are genetically linked to Fe-S cluster assembly and specific respiratory pathways. Systematic analysis of mutant strains of ravA and viaA indicated that RavA-ViaA sensitizes cells to sublethal concentrations of aminoglycosides. Furthermore, this effect was dependent on RavA's ATPase activity, and on the presence of specific subunits of NADH:ubiquinone oxidoreductase I (Nuo Complex, or Complex I). Importantly, both RavA and ViaA were found to physically interact with specific Nuo subunits. We propose that RavA-ViaA facilitate the maturation of the Nuo complex. |
format | Online Article Text |
id | pubmed-3893208 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-38932082014-01-21 The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli Wong, Keith S. Snider, Jamie D. Graham, Chris Greenblatt, Jack F. Emili, Andrew Babu, Mohan Houry, Walid A. PLoS One Research Article MoxR ATPases are widespread throughout bacteria and archaea. The experimental evidence to date suggests that these proteins have chaperone-like roles in facilitating the maturation of dedicated protein complexes that are functionally diverse. In Escherichia coli, the MoxR ATPase RavA and its putative cofactor ViaA are found to exist in early stationary-phase cells at 37°C at low levels of about 350 and 90 molecules per cell, respectively. Both proteins are predominantly localized to the cytoplasm, but ViaA was also unexpectedly found to localize to the cell membrane. Whole genome microarrays and synthetic lethality studies both indicated that RavA-ViaA are genetically linked to Fe-S cluster assembly and specific respiratory pathways. Systematic analysis of mutant strains of ravA and viaA indicated that RavA-ViaA sensitizes cells to sublethal concentrations of aminoglycosides. Furthermore, this effect was dependent on RavA's ATPase activity, and on the presence of specific subunits of NADH:ubiquinone oxidoreductase I (Nuo Complex, or Complex I). Importantly, both RavA and ViaA were found to physically interact with specific Nuo subunits. We propose that RavA-ViaA facilitate the maturation of the Nuo complex. Public Library of Science 2014-01-15 /pmc/articles/PMC3893208/ /pubmed/24454883 http://dx.doi.org/10.1371/journal.pone.0085529 Text en © 2014 Wong et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Wong, Keith S. Snider, Jamie D. Graham, Chris Greenblatt, Jack F. Emili, Andrew Babu, Mohan Houry, Walid A. The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli |
title | The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli
|
title_full | The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli
|
title_fullStr | The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli
|
title_full_unstemmed | The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli
|
title_short | The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli
|
title_sort | moxr atpase rava and its cofactor viaa interact with the nadh:ubiquinone oxidoreductase i in escherichia coli |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3893208/ https://www.ncbi.nlm.nih.gov/pubmed/24454883 http://dx.doi.org/10.1371/journal.pone.0085529 |
work_keys_str_mv | AT wongkeiths themoxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT sniderjamied themoxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT grahamchris themoxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT greenblattjackf themoxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT emiliandrew themoxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT babumohan themoxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT hourywalida themoxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT wongkeiths moxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT sniderjamied moxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT grahamchris moxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT greenblattjackf moxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT emiliandrew moxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT babumohan moxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli AT hourywalida moxratpaseravaanditscofactorviaainteractwiththenadhubiquinoneoxidoreductaseiinescherichiacoli |