Efficient cleavage of problematic tobacco etch virus (TEV)-protein arginine methyltransferase constructs

Brenda B. Suh-Lailam, Joan M. Hevel*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Protein arginine methyltransferases (PRMTs) are enzymes that are involved in many biological processes. Several studies have shown that the identity of the N-terminal fusion tag affects the substrate selectivity of PRMTs. Therefore, to accurately study substrate recognition, it is imperative that a tagless PRMT be used. However, cleavage of tagged PRMTs has been problematic. We have developed a successful method by which untagged PRMTs can be made using a tobacco etch virus (TEV) cleavage site at the N-terminal domain. This method may be useful for cleaving other challenging target proteins that have the TEV protease recognition site.

Original languageEnglish (US)
Pages (from-to)130-132
Number of pages3
JournalAnalytical Biochemistry
Volume387
Issue number1
DOIs
StatePublished - Apr 1 2009

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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