Elongation factor Tu is a multifunctional and processed moonlighting protein

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Widjaja, Michael, Harvey, Kate Louise, Hagemann, Lisa, Berry, Iain James, Jarocki, Veronica Maria, Raymond, Benjamin Bernard Armando, Tacchi, Jessica Leigh, Gründel, Anne, Steele, Joel Ricky, Padula, Matthew Paul, Charles, Ian George, Dumke, Roger and Djordjevic, Steven Philip (2017) Elongation factor Tu is a multifunctional and processed moonlighting protein. Scientific Reports, 7. ISSN 2045-2322

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Abstract

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.

Item Type: Article
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
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Depositing User: Pure Connector
Date Deposited: 20 Sep 2017 05:06
Last Modified: 21 Oct 2022 16:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/64929
DOI: 10.1038/s41598-017-10644-z

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