Mass spectrometry data confirming tetrameric ?-synuclein N-terminal acetylation.

ABSTRACT: Tetrameric ?-synuclein (?S) is an elusive multimer of the dynamic neuronal protein implicated in Parkinson?s disease. Through the data reported herein, we demonstrate that this high molecular weight multimer is N-acetylated. Coexpression of tetrameric ?S in Escherichia coli with the NatB acetylase derived from yeast enables access to N-terminally acetylated ?S (^NAc?S), the native form in humans. Following purification and characterization as previously described by us in "Isolation of Recombinant Tetrameric N-acetylated ?-synuclein" (Fernández and Lucas, 2018), the purified protein was excised from a native gel for confirmation of N-terminal acetylation. Through high-resolution mass spectrometry techniques, the identification of this helical tetramer as ^NAc?S has been clearly demonstrated.

SUBMITTER: Fernandez RD 

PROVIDER: S-EPMC6157607 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature