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J Proteomics. 2015 Aug 3;126:296-302. doi: 10.1016/j.jprot.2015.05.022. Epub 2015 May 26.

Beyond single modification: Reanalysis of the acetylproteome of human sperm reveals widespread multiple modifications.

Author information

1
State Key Laboratory of Reproductive Medicine, Nanjing Medical University, Nanjing 210029, PR China. Electronic address: zhoutao@njmu.edu.cn.
2
State Key Laboratory of Reproductive Medicine, Nanjing Medical University, Nanjing 210029, PR China.
3
State Key Laboratory of Reproductive Medicine, Nanjing Medical University, Nanjing 210029, PR China. Electronic address: xrwang@njmu.edu.cn.

Abstract

Sperm is an ideal model for studying post-translational modifications since its transcriptional and translational activities are nearly silent. Thus, sperm functions are mainly regulated at the protein level, especially by means of post-translational modifications. Published proteomic datasets may contain valuable undiscovered information. In this study, we reanalyzed the raw data from previous acetylproteome study on human capacitated sperm to include two additional modifications: phosphorylation and ubiquitination. We successfully identified approximately 500 proteins with multiple types of modifications. Compared with recently developed serial enrichment strategy for multiple modifications, reanalysis of single modification enriched data provides a direct and efficient alternative approach. These results greatly expand our knowledge of protein modifications in human sperm.

KEYWORDS:

Acetylation; Human sperm; Post-translational modification; Reanalysis; Tandem proteomics

PMID:
26021710
DOI:
10.1016/j.jprot.2015.05.022
[Indexed for MEDLINE]

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