TY - JOUR
T1 - Efficient cleavage of problematic tobacco etch virus (TEV)-protein arginine methyltransferase constructs
AU - Suh-Lailam, Brenda B.
AU - Hevel, Joan M.
PY - 2009/4/1
Y1 - 2009/4/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.ab.2008.12.031
DO - 10.1016/j.ab.2008.12.031
M3 - Article
C2 - 19167339
AN - SCOPUS:60549102431
SN - 0003-2697
VL - 387
SP - 130
EP - 132
JO - Analytical Biochemistry
JF - Analytical Biochemistry
IS - 1
ER -