In vivomethylation of OLA1 revealed by activity-based target profiling of NTMT1
| Autor: | Wei Wu, Gaochao Huang, Kaimin Jia, Yulan Xiong, Ruben Shrestha, Ping Li, Bingbing Wu |
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| Rok vydání: | 2019 |
| Předmět: |
Signal peptide
Methionine biology 010405 organic chemistry ATPase Cellular functions A protein General Chemistry Methylation 010402 general chemistry 01 natural sciences 0104 chemical sciences 3. Good health chemistry.chemical_compound Biochemistry chemistry In vivo Methyltransferase 1 biology.protein |
| Zdroj: | Chemical Science. 10:8094-8099 |
| ISSN: | 2041-6539 2041-6520 |
| DOI: | 10.1039/c9sc02550b |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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