Acetylation in Borrelia burgdorferi
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Elite
ORGANISM(S): Borrelia Burgdorferi B31
SUBMITTER: 
Julie Hardouin
LAB HEAD: Julie Hardouin
PROVIDER: PXD010065 | Pride | 2018-09-24
REPOSITORIES: Pride
Publications
Global Profiling of Lysine Acetylation in <i>Borrelia burgdorferi</i> B31 Reveals Its Role in Central Metabolism.
Bontemps-Gallo Sébastien S Gaviard Charlotte C Richards Crystal L CL Kentache Takfarinas T Raffel Sandra J SJ Lawrence Kevin A KA Schindler Joseph C JC Lovelace Joseph J Dulebohn Daniel P DP Cluss Robert G RG Hardouin Julie J Gherardini Frank C FC
Frontiers in microbiology 20180831
The post-translational modification of proteins has been shown to be extremely important in prokaryotes. Using a highly sensitive mass spectrometry-based proteomics approach, we have characterized the acetylome of <i>B. burgdorferi</i>. As previously reported for other bacteria, a relatively low number (5%) of the potential genome-encoded proteins of <i>B. burgdorferi</i> were acetylated. Of these, the vast majority were involved in central metabolism and cellular information processing (transcr ...[more]
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