PMID: 8604339Mar 15, 1996Paper

Interaction of tRNA (uracil-5-)-methyltransferase with NO2Ura-tRNA

Nucleic Acids Research
X GuD V Santi

Abstract

tRNA in which uracil is completely replaced by 5-nitro-uracil was prepared by substituting 5-nitro-UTP for UTP in an in vitro transcription reaction. The rationale was that the 5-nitro substituent activates the 6-carbon of the Ura heterocycle towards nucleophiles, and hence could provide mechanism-based inhibitors of enzymes which utilize this feature in their catalytic mechanism. When assayed shortly after mixing, the tRNA analog, NO2Ura-tRNA, is a potent competitive inhibitor of tRNA-Ura methyl transferase (RUMT). Upon incubation, the analog causes a time-dependent inactivation of RUMT which could be reversed by dilution into a large excess of tRNA substrate. Covalent RUMT-NO2Ura-tRNA complexes could be isolated on nitrocellulose filters or by SDS-PAGE. The interaction of RUMT and NO2Ura-tRNA was deduced to involve formation of a reversible complex, followed by formation of a reversible covalent complex in which Cys 324 of RUMT is linked to the 6-position of NO2Ura 54 in NO2Ura-tRNA.

References

Feb 1, 1991·Protein Expression and Purification·X Gu, D V Santi
May 1, 1990·DNA and Cell Biology·X R Gu, D V Santi
Feb 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·J R Sampson, O C Uhlenbeck

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Citations

Oct 26, 2012·The Journal of Biological Chemistry·Ryota YamagamiHiroyuki Hori
Aug 6, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·William H Gmeiner

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