Acetylome and propionylome of Acinetobacter baumannii SK17
Date Issued
2015
Date
2015
Author(s)
Tsai, Cheng-Han
Abstract
Lysine acetylation is one of the most prevalent post-translational modifications (PTMs) detected in both eukaryotes and bacteria. Recently, many acetylproteins have been reported to play pivotal roles in various cellular processes in eukaryotes. However, the function and extent of this modification in prokaryotic cells remain largely unexplored. Besides, another novel lysine modification, lysine propionylation, is potential to have important functions in the regulation of biological processes. In this study, by using a mass spectrometry-based proteomic approach in combination with immunoprecipitation, we identified 174/ 96 lysine acetylation/ propionylation sites from 128/ 71 acetyl-/ propionylproteins in clinical isolates of Acinetobacter baumannii SK17. The bioinformatics analysis of both acetylome and propionylome showed that the identified proteins were involved in diverse cellular functions including nucleotide metabolism, amino acid metabolism, carbohydrate metabolism, membrane transporter and stress response. To further characterize the definite effects of these PTMs on proteins, we examined the identification of lysine-modified peptides based on their homologous protein structures. Among these, DNA-binding protein HU (also known as nucleoid-associated protein HU), a small dimeric protein, playing a critical role in maintenance of chromosomal architecture and various DNA transactions, was acetylated on Lys-13. In addition, we further proved this acetylated site would influence the stability of quaternary structure of HU protein and decrease its DNA binding ability. Our findings demonstrated that lysine acetylation and propinylation are abundant in A. baumannii SK17 and provide an in-depth exploration of the biological functions on lysine acetylated and propionylated proteins.
Subjects
lysine acetylation
lysine propionylation
A. baumannii SK17
DNA-binding protein HU-β
Type
thesis