Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation.
Elongation factor RbbA is required for ATP-dependent deacyl-tRNA release presumably after each peptide bond formation; however, there is no information about the cellular role. Proteomic analysis in Escherichia coli revealed that RbbA reciprocally co-purified with a conserved inner membrane protein...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2011-04-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0018510&type=printable |
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| author | Mohan Babu Hiroyuki Aoki Wasimul Q Chowdhury Alla Gagarinova Chris Graham Sadhna Phanse Ben Laliberte Noor Sunba Matthew Jessulat Ashkan Golshani Andrew Emili Jack F Greenblatt M Clelia Ganoza |
| author_facet | Mohan Babu Hiroyuki Aoki Wasimul Q Chowdhury Alla Gagarinova Chris Graham Sadhna Phanse Ben Laliberte Noor Sunba Matthew Jessulat Ashkan Golshani Andrew Emili Jack F Greenblatt M Clelia Ganoza |
| author_sort | Mohan Babu |
| collection | DOAJ |
| description | Elongation factor RbbA is required for ATP-dependent deacyl-tRNA release presumably after each peptide bond formation; however, there is no information about the cellular role. Proteomic analysis in Escherichia coli revealed that RbbA reciprocally co-purified with a conserved inner membrane protein of unknown function, YhjD. Both proteins are also physically associated with the 30S ribosome and with members of the lipopolysaccharide transport machinery. Genome-wide genetic screens of rbbA and yhjD deletion mutants revealed aggravating genetic interactions with mutants deficient in the electron transport chain. Cells lacking both rbbA and yhjD exhibited reduced cell division, respiration and global protein synthesis as well as increased sensitivity to antibiotics targeting the ETC and the accuracy of protein synthesis. Our results suggest that RbbA appears to function together with YhjD as part of a regulatory network that impacts bacterial oxidative phosphorylation and translation efficiency. |
| format | Article |
| id | doaj-art-17514a7b656746b6b4282c075d3f8fc5 |
| institution | Kabale University |
| issn | 1932-6203 |
| language | English |
| publishDate | 2011-04-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-17514a7b656746b6b4282c075d3f8fc52025-08-20T03:31:05ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-04-0164e1851010.1371/journal.pone.0018510Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation.Mohan BabuHiroyuki AokiWasimul Q ChowdhuryAlla GagarinovaChris GrahamSadhna PhanseBen LaliberteNoor SunbaMatthew JessulatAshkan GolshaniAndrew EmiliJack F GreenblattM Clelia GanozaElongation factor RbbA is required for ATP-dependent deacyl-tRNA release presumably after each peptide bond formation; however, there is no information about the cellular role. Proteomic analysis in Escherichia coli revealed that RbbA reciprocally co-purified with a conserved inner membrane protein of unknown function, YhjD. Both proteins are also physically associated with the 30S ribosome and with members of the lipopolysaccharide transport machinery. Genome-wide genetic screens of rbbA and yhjD deletion mutants revealed aggravating genetic interactions with mutants deficient in the electron transport chain. Cells lacking both rbbA and yhjD exhibited reduced cell division, respiration and global protein synthesis as well as increased sensitivity to antibiotics targeting the ETC and the accuracy of protein synthesis. Our results suggest that RbbA appears to function together with YhjD as part of a regulatory network that impacts bacterial oxidative phosphorylation and translation efficiency.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0018510&type=printable |
| spellingShingle | Mohan Babu Hiroyuki Aoki Wasimul Q Chowdhury Alla Gagarinova Chris Graham Sadhna Phanse Ben Laliberte Noor Sunba Matthew Jessulat Ashkan Golshani Andrew Emili Jack F Greenblatt M Clelia Ganoza Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation. PLoS ONE |
| title | Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation. |
| title_full | Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation. |
| title_fullStr | Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation. |
| title_full_unstemmed | Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation. |
| title_short | Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation. |
| title_sort | ribosome dependent atpase interacts with conserved membrane protein in escherichia coli to modulate protein synthesis and oxidative phosphorylation |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0018510&type=printable |
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