Elongation factor Tu is a multifunctional and processed moonlighting protein

Widjaja, M; Harvey, KL; Hagemann, L; Berry, IJ; Jarocki, VM; Raymond, BBA; Tacchi, JL; Gründel, A; Steele, JR; Padula, MP; Charles, IG; Dumke, R; Djordjevic, SP

Elongation factor Tu is a multifunctional and processed moonlighting protein

Widjaja, M

Harvey, KL Hagemann, L Berry, IJ

Jarocki, VM

Raymond, BBA

Tacchi, JL Gründel, A Steele, JR

Padula, MP

Charles, IG

Dumke, R Djordjevic, SP

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Publication Type:: Journal Article
Citation:: Scientific Reports, 2017, 7 (1)
Issue Date:: 2017-12-01

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Field	Value	Language
dc.contributor.author	Widjaja, M https://orcid.org/0000-0003-1509-0443	en_US
dc.contributor.author	Harvey, KL	en_US
dc.contributor.author	Hagemann, L	en_US
dc.contributor.author	Berry, IJ https://orcid.org/0000-0002-0322-2595	en_US
dc.contributor.author	Jarocki, VM https://orcid.org/0000-0003-1249-0994	en_US
dc.contributor.author	Raymond, BBA https://orcid.org/0000-0003-3610-9289	en_US
dc.contributor.author	Tacchi, JL	en_US
dc.contributor.author	Gründel, A	en_US
dc.contributor.author	Steele, JR https://orcid.org/0000-0002-3070-9761	en_US
dc.contributor.author	Padula, MP https://orcid.org/0000-0002-8283-0643	en_US
dc.contributor.author	Charles, IG https://orcid.org/0000-0002-2423-1167	en_US
dc.contributor.author	Dumke, R	en_US
dc.contributor.author	Djordjevic, SP https://orcid.org/0000-0001-9301-5372	en_US
dc.date.available	2017-08-10	en_US
dc.date.issued	2017-12-01	en_US
dc.identifier.citation	Scientific Reports, 2017, 7 (1)	en_US
dc.identifier.uri	http://hdl.handle.net/10453/120531
dc.description.abstract	© 2017 The Author(s). Many bacterial moonlighting proteins were originally described in medically, agriculturally, and commercially important members of the low G + C Firmicutes. We show Elongation factor Tu (Ef-Tu) moonlights on the surface of the human pathogens Staphylococcus aureus (SaEf-Tu) and Mycoplasma pneumoniae (MpnEf-Tu), and the porcine pathogen Mycoplasma hyopneumoniae (MhpEf-Tu). Ef-Tu is also a target of multiple processing events on the cell surface and these were characterised using an N-terminomics pipeline. Recombinant MpnEf-Tu bound strongly to a diverse range of host molecules, and when bound to plasminogen, was able to convert plasminogen to plasmin in the presence of plasminogen activators. Fragments of Ef-Tu retain binding capabilities to host proteins. Bioinformatics and structural modelling studies indicate that the accumulation of positively charged amino acids in short linear motifs (SLiMs), and protein processing promote multifunctional behaviour. Codon bias engendered by an A + T rich genome may influence how positively-charged residues accumulate in SLiMs.	en_US
dc.relation	http://purl.org/au-research/grants/arc/LE130100096
dc.relation.ispartof	Scientific Reports	en_US
dc.relation.isbasedon	10.1038/s41598-017-10644-z	en_US
dc.subject.mesh	Mycoplasma hyopneumoniae	en_US
dc.subject.mesh	Mycoplasma pneumoniae	en_US
dc.subject.mesh	Staphylococcus aureus	en_US
dc.subject.mesh	Plasminogen	en_US
dc.subject.mesh	Peptide Elongation Factor Tu	en_US
dc.subject.mesh	Membrane Proteins	en_US
dc.subject.mesh	Virulence Factors	en_US
dc.subject.mesh	Computational Biology	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	Host-Pathogen Interactions	en_US
dc.subject.mesh	Fibrinolysin	en_US
dc.title	Elongation factor Tu is a multifunctional and processed moonlighting protein	en_US
dc.type	Journal Article
utslib.citation.volume	1	en_US
utslib.citation.volume	7	en_US
utslib.for	0304 Medicinal and Biomolecular Chemistry	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Provost
pubs.organisational-group	/University of Technology Sydney/Provost/Jumbunna
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	open_access
pubs.issue	1	en_US
pubs.publication-status	Published	en_US
pubs.volume	7	en_US

Abstract:

© 2017 The Author(s). Many bacterial moonlighting proteins were originally described in medically, agriculturally, and commercially important members of the low G + C Firmicutes. We show Elongation factor Tu (Ef-Tu) moonlights on the surface of the human pathogens Staphylococcus aureus (SaEf-Tu) and Mycoplasma pneumoniae (MpnEf-Tu), and the porcine pathogen Mycoplasma hyopneumoniae (MhpEf-Tu). Ef-Tu is also a target of multiple processing events on the cell surface and these were characterised using an N-terminomics pipeline. Recombinant MpnEf-Tu bound strongly to a diverse range of host molecules, and when bound to plasminogen, was able to convert plasminogen to plasmin in the presence of plasminogen activators. Fragments of Ef-Tu retain binding capabilities to host proteins. Bioinformatics and structural modelling studies indicate that the accumulation of positively charged amino acids in short linear motifs (SLiMs), and protein processing promote multifunctional behaviour. Codon bias engendered by an A + T rich genome may influence how positively-charged residues accumulate in SLiMs.

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http://hdl.handle.net/10453/120531