Findings from University of Minnesota Twin Cities Reveals New Findings on Life Science (A Constitutional Isomer Selective Chemical Proteomic Strategy for System-wide Profiling of Protein Lysine 5-hydroxylation).

Researchers at the University of Minnesota Twin Cities have developed a chemical proteomic strategy to identify protein lysine 5-hydroxylation (5-Hyl) using highly selective periodate chemistry. This method allowed for the identification of over 1600 5-Hyl sites on 630 proteins in human cells, shedding light on the functional significance of this modification in protein structure, transcription, and chromatin regulation. The study also revealed insights into the role of Jumonji-domain containing protein 6 (JMJD6) in regulating 5-Hyl proteins through alternative splice isoforms, providing unique perspectives on transcriptional regulation and cellular development. This research was funded by the NIH National Institute of General Medical Sciences (NIGMS) and the National Institutes of Health (NIH) in the USA. [Extracted from the article]