Journal
CHEMICAL SCIENCE
Volume 10, Issue 35, Pages 8094-8099Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9sc02550b
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Funding
- NIH [R01GM117259-S1, P30GM110761]
- Johnson Cancer Centre Innovative Research Award
- Dane G. Hansen Graduate Fellowship
- K-INBRE postdoctoral fellowship under NIH [P20GM103418]
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N-Terminal methyltransferase 1 (NTMT1) catalyzes the N-terminal methylation of proteins with a specific-N-terminal motif after methionine removal. Aberrant N-terminal methylation has been implicated in several cancers and developmental diseases. Together with motif sequence and signal peptide analyses, activity-based substrate profiling of NTMT1 utilizing (E)-hex-2-en-5-ynyl-S-adenosyl-L-methionine (Hey-SAM) revealed 72 potential targets, which include several previously confirmed ones and many unknowns. Target validation using normal and NTMT1 knock-out (KO) HEK293FT cells generated by CRISPR-Cas9 demonstrated that Obg-like ATPase 1 (OLA1), a protein involved in many critical cellular functions, is methylated in vivo by NTMT1. Additionally, Hey-SAM synthesis achieved >= 98% yield for SAH conversion.
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