Lysine acetylation is a common post-translational modification of key metabolic pathway enzymes of the anaerobe Porphyromonas gingivalis

Journal of Proteomics
Catherine A ButlerEric C Reynolds

Abstract

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 identified 130 lysine acetylated peptides from 92 P. gingivalis proteins. The majority of these peptides (71) were attributed to 45 proteins with predicted metabolic activity; these proteins could be mapped to several P. gingivalis metabolic pathways where enzymes catalysing sequential reactions within the same pathway were often found acetylated. In particular, the catabolic pathways of complex anaerobic fermentation of amino acids to produce energy had 12 enzymes lysine acetylated. The results suggest that lysine acetylation may be an impor...Continue Reading

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Dec 21, 2016·Proteomics·Nagihan Bostanci, Kai Bao
Sep 27, 2018·Journal of Bacteriology·Arunima MishraHansel M Fletcher
Feb 21, 2019·Journal of Bacteriology·Birgit SchillingChristopher V Rao
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Jul 11, 2018·Journal of Oral Microbiology·Yuqing LiMargaret J Duncan
Aug 25, 2021·MSystems·Jackson Luu, Valerie J Carabetta

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