Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation.

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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Main Authors: 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
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-04-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0018510&type=printable
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