Leveraging Immonium Ions for Targeting Acyl-Lysine Modifications in Proteomic Datasets.

Leveraging Immonium Ions for Targeting Acyl-Lysine Modifications in Proteomic Datasets.
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DOI:
10.1002/pmic.202000111
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发表时间:
2021-03
期刊:
影响因子:
3.4
通讯作者:
Loo JA
Loo JA
中科院分区:
生物学3区
文献类型:
--
作者:
Muroski JM;Fu JY;Nguyen HH;Ogorzalek Loo RR;Loo JA

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Acyl modifications vary greatly in terms of elemental composition and site of protein modification. Developing methods to identify acyl modifications more confidently can help to assess the scope of these modifications in large proteomic datasets. We analyze the utility of acyl-lysine immonium ions for identifying the modifications in proteomic datasets. We demonstrate that the cyclized immonium ion is a strong indicator of acyl-lysine presence when its rank or relative abundance compared to other ions within a spectrum is considered. Utilizing a stepped collision energy method in a shotgun experiment highlights the immonium ion strongly. By implementing an analysis that accounted for features within each MS2 spectrum, the method clearly identified peptides with short chain acyl-lysine modifications from complex lysates. Immonium ions can also be used to validate novel acyl-modifications; in this study we report the first examples of 3-hydroxylpimelyl-lysine modifications and validate them using immonium ions. Overall these results solidify the use of the immonium ion as a marker for acyl-lysine modifications in complex proteomic datasets.
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