A Chemical Probe for Lysine Malonylation

Authors


  • We thank Prof. Chi-Ming Che for generous support on the mass spectrometer, Prof. Dan Yang for advice and support, Prof. Quan Hao for useful discussions, and Di Hu for technical assistance. X.D.L. acknowledges a seed fund from The University of Hong Kong (201111159240) and Hung Hing Ying Physical Science Research Fund (20373739). Y.M.E.F. thanks the Small Project Funding from The University of Hong Kong (201109176193) and the Special Equipment Grant from the University Grants Committee of the Hong Kong Special Administrative Region, China (Project Code: SEG_HKU02).

Abstract

original image

Tag! You′re it! MalAM-yne is a chemical reporter for malonylation of lysines within proteins (see scheme), a newly identified posttranslational modification. MalAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent bioorthogonal tag conjugation allows the fluorescent visualization of cellular malonylation and profiling of malonylated proteins.

Ancillary