High-Throughput Screening of Sulfated Proteins by Using a Genome-Wide Proteome Microarray and Protein Tyrosine Sulfation System

Bo Yu Huang, Po Chung Chen, Bo Han Chen, Chen Chu Wang, Hsuan Fu Liu, Yi Zao Chen, Chien Sheng Chen*, Yuh-Shyong Yang

*Corresponding author for this work

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Protein tyrosine sulfation (PTS) is a widespread posttranslational modification that induces intercellular and extracellular responses by regulating protein-protein interactions and enzymatic activity. Although PTS affects numerous physiological and pathological processes, only a small fraction of the total predicted sulfated proteins has been identified to date. Here, we localized the potential sulfation sites of Escherichia coli proteins on a proteome microarray by using a 3′-phosphoadenosine 5′-phosphosulfate (PAPS) synthase-coupled tyrosylprotein sulfotransferase (TPST) catalysis system that involves in situ PAPS generation and TPST catalysis. Among the 4256 E. coli K12 proteins, 875 sulfated proteins were identified using antisulfotyrosine primary and Cy3-labeled antimouse secondary antibodies. Our findings add considerably to the list of potential proteins subjected to tyrosine sulfation. Similar procedures can be applied to identify sulfated proteins in yeast and human proteome microarrays, and we expect such approaches to contribute substantially to the understanding of important human diseases. (Figure Presented).

Original languageEnglish
Pages (from-to)3278-3284
Number of pages7
JournalAnalytical Chemistry
Volume89
Issue number6
DOIs
StatePublished - 21 Mar 2017

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