The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G

Biswaranjan Mohanty, Paulina Hanson-Manful, Thomas J. Finn, Cecilia R. Chambers, James L.O. McKellar, Ingrid Macindoe, Stephanie Helder, Surya Setiyaputra, Yichen Zhong, Joel P. Mackay, Wayne M. Patrick

Research output: Contribution to journalArticleResearchpeer-review

Abstract

InterPro family IPR020489 comprises ~1000 uncharacterized bacterial proteins. Previously we showed that overexpressing the Escherichia coli representative of this family, EcYejG, conferred low-level resistance to aminoglycoside antibiotics. In an attempt to shed light on the biochemical function of EcYejG, we have solved its structure using multinuclear solution NMR spectroscopy. The structure most closely resembles that of domain III from elongation factor G (EF-G). EF-G catalyzes ribosomal translocation and mutations in EF-G have also been associated with aminoglycoside resistance. While we were unable to demonstrate a direct interaction between EcYejG and the ribosome, the protein might play a role in translation.

Original languageEnglish
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
DOIs
Publication statusAccepted/In press - 8 Apr 2019

Keywords

  • aminoglycoside
  • elongation factor
  • IPR020489
  • NMR
  • PF13989
  • RNA recognition motif

Cite this

Mohanty, Biswaranjan ; Hanson-Manful, Paulina ; Finn, Thomas J. ; Chambers, Cecilia R. ; McKellar, James L.O. ; Macindoe, Ingrid ; Helder, Stephanie ; Setiyaputra, Surya ; Zhong, Yichen ; Mackay, Joel P. ; Patrick, Wayne M. / The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G. In: Proteins: Structure, Function and Bioinformatics. 2019.
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abstract = "InterPro family IPR020489 comprises ~1000 uncharacterized bacterial proteins. Previously we showed that overexpressing the Escherichia coli representative of this family, EcYejG, conferred low-level resistance to aminoglycoside antibiotics. In an attempt to shed light on the biochemical function of EcYejG, we have solved its structure using multinuclear solution NMR spectroscopy. The structure most closely resembles that of domain III from elongation factor G (EF-G). EF-G catalyzes ribosomal translocation and mutations in EF-G have also been associated with aminoglycoside resistance. While we were unable to demonstrate a direct interaction between EcYejG and the ribosome, the protein might play a role in translation.",
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Mohanty, B, Hanson-Manful, P, Finn, TJ, Chambers, CR, McKellar, JLO, Macindoe, I, Helder, S, Setiyaputra, S, Zhong, Y, Mackay, JP & Patrick, WM 2019, 'The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G' Proteins: Structure, Function and Bioinformatics. https://doi.org/10.1002/prot.25687

The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G. / Mohanty, Biswaranjan; Hanson-Manful, Paulina; Finn, Thomas J.; Chambers, Cecilia R.; McKellar, James L.O.; Macindoe, Ingrid; Helder, Stephanie; Setiyaputra, Surya; Zhong, Yichen; Mackay, Joel P.; Patrick, Wayne M.

In: Proteins: Structure, Function and Bioinformatics, 08.04.2019.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Helder, Stephanie

AU - Setiyaputra, Surya

AU - Zhong, Yichen

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AU - Patrick, Wayne M.

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