title: A glimpse into the modulation of post-translational modifications of human-colonizing bacteria.
abstract: Protein post-translational modifications (PTMs) are a key bacterial feature that holds the capability to modulate protein function and responses to environmental cues. Until recently, their role in the regulation of prokaryotic systems has been largely neglected. However, the latest developments in mass spectrometry-based proteomics have allowed an unparalleled identification and quantification of proteins and peptides that undergo PTMs in bacteria, including in species which directly or indirectly affect human health. Herein, we address this issue by carrying out the largest and most comprehensive global pooling and comparison of PTM peptides and proteins from bacterial species performed to date. Data was collected from 91 studies relating to PTM bacterial peptides or proteins identified by mass spectrometry-based methods. The present analysis revealed that there was a considerable overlap between PTMs across species, especially between acetylation and other PTMs, particularly succinylation. Phylogenetically closer species may present more overlapping phosphoproteomes, but environmental triggers also contribute to this proximity. PTMs among bacteria were found to be extremely versatile and diverse, meaning that the same protein may undergo a wide variety of different modifications across several species, but it could also suffer different modifications within the same species.
authors.affiliation: Department of Medical Sciences, Institute for Biomedicine-iBiMED, University of Aveiro, Aveiro, Portugal; Department of Chemistry, University of Aveiro, Portugal.
authors.forename: Paulo André Dias
authors.initials: PAD
authors.lastname: Bastos
authors.affiliation: CESAM, Department of Chemistry, University of Aveiro, Portugal. Electronic address: jpintocosta@ua.pt.
authors.forename: João Pinto
authors.initials: JP
authors.lastname: da Costa
authors.affiliation: Department of Medical Sciences, Institute for Biomedicine-iBiMED, University of Aveiro, Aveiro, Portugal; Department of Physiology and Cardiothoracic Surgery, Faculty of Medicine, University of Porto, Porto, Portugal. Electronic address: rvitorino@ua.pt.
authors.forename: Rui
authors.initials: R
authors.lastname: Vitorino
mesh_terms: D000107:Acetylation; D001419:Bacteria / Q000737:chemistry*; D001426:Bacterial Proteins / Q000378:metabolism*; D003625:Data Collection / Q000379:methods; D006801:Humans; D013058:Mass Spectrometry; D010455:Peptides / Q000378:metabolism; D010750:Phosphoproteins; D010766:Phosphorylation; D010802:Phylogeny; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods; D019802:Succinic Acid / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D010455:Peptides; D010750:Phosphoproteins; D019802:Succinic Acid
keywords: Acetylation; Antibiotic resistant; Bacterial protein; Glycosylation; Lipidation; Mass spectrometry; Multi-resistance; Phosphorylation; Post-translational modification; Succinylation