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Cell Chem Biol. 2018 Nov 15;25(11):1380-1388.e4. doi: 10.1016/j.chembiol.2018.08.006. Epub 2018 Aug 30.

Selenocysteine-Specific Mass Spectrometry Reveals Tissue-Distinct Selenoproteomes and Candidate Selenoproteins.

Author information

1
Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Road, Pudong, Shanghai 201210, China; University of Chinese Academy of Sciences, Beijing 100049, China.
2
Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Road, Pudong, Shanghai 201210, China.
3
Departments of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
4
Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Road, Pudong, Shanghai 201210, China. Electronic address: zyy@sioc.ac.cn.

Abstract

Selenoproteins, defined by the presence of selenocysteines (Sec), play important roles in a wide range of biological processes. All known selenoproteins are marked by the presence of Sec insertion sequence (SECIS) at their mRNA. The lack of an effective analytical method has hindered our ability to explore the selenoproteome and new selenoproteins beyond SECIS. Here, we develop a Sec-specific mass spectrometry-based technique, termed "SecMS," which allows the systematic profiling of selenoproteomes by selective alkylation of Sec. Using SecMS, we quantitatively characterized the age- and stress-regulated selenoproteomes for nine tissues from mice of different ages and mammalian cells, demonstrating tissue-specific selenoproteomes and an age-dependent decline in specific selenoproteins in brains and hearts. We established an integrated platform using SecMS and SECIS-independent selenoprotein (SIS) database and further identified five candidate selenoproteins. The application of this integrated platform provides an effective strategy to explore the selenoproteome independent of SECIS.

KEYWORDS:

Sec-specific mass spectrometry (SecMS); alkylation; quantitative proteomics; selenocysteine; selenoprotein; selenoproteomes

PMID:
30174312
DOI:
10.1016/j.chembiol.2018.08.006
[Indexed for MEDLINE]

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