Lysine acetylation is a common post-translational modification of key metabolic pathway enzymes of the anaerobe Porphyromonas gingivalis
Catherine A Butler, Paul D Veith, Matthew F Nieto, Stuart G Dashper, Eric C Reynolds
JOURNAL OF PROTEOMICS | ELSEVIER | Published : 2015
Porphyromonas gingivalis is a Gram-negative anaerobe considered to be a keystone pathogen in the development of the bacterial-associated inflammatory oral disease chronic periodontitis. Although post-translational modifications (PTMs) of proteins are commonly found to modify protein function in eukaryotes and prokaryotes, PTMs such as lysine acetylation have not been examined in P. gingivalis. Lysine acetylation is the addition of an acetyl group to a lysine which removes this amino acid's positive charge and can induce changes in a protein's secondary structure and reactivity. A proteomics based approach combining immune-affinity enrichment with high sensitivity Orbitrap mass spectrometry i..View full abstract
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Awarded by Australian Dental Research Foundation
The Orbitrap mass spectrometry was performed by Dr. Ching Seng Ang at the Mass Spectrometry and Proteomics Facility of the Bio21 Molecular Science and Biotechnology Institute, Melbourne, Australia. This research was supported by the Australian Dental Research Foundation grant 34-2014.