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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

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

Fernández Ricardo D RD   Lucas Heather R HR  

Data in brief 20180914


Tetrameric α-synuclein (αS) 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 αS in <i>Escherichia coli</i> with the NatB acetylase derived from yeast enables access to N-terminally acetylated αS (<sup>NAc</sup>αS), the native form in humans. Following purification and characterization as previously described by us in "Isola  ...[more]

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