TY - JOUR
T1 - Archaeal Elp3 catalyzes tRNA wobble uridine modification at C5 via a radical mechanism
AU - Selvadurai, Kiruthika
AU - Wang, Pei
AU - Seimetz, Joseph
AU - Huang, Raven H.
N1 - Publisher Copyright:
© 2014 Nature America, Inc. All rights reserved.
PY - 2014/10/1
Y1 - 2014/10/1
N2 - Approximately 25% of cytoplasmic tRNAs in eukaryotic organisms have the wobble uridine (U34) modified at C5 through a process that, according to genetic studies, is carried out by the eukaryotic Elongator complex. Here we show that a single archaeal protein, the homolog of the third subunit of the eukaryotic Elongator complex (Elp3), is able to catalyze the same reaction. The mechanism of action by Elp3 described here represents unprecedented chemistry performed on acetyl-CoA.
AB - Approximately 25% of cytoplasmic tRNAs in eukaryotic organisms have the wobble uridine (U34) modified at C5 through a process that, according to genetic studies, is carried out by the eukaryotic Elongator complex. Here we show that a single archaeal protein, the homolog of the third subunit of the eukaryotic Elongator complex (Elp3), is able to catalyze the same reaction. The mechanism of action by Elp3 described here represents unprecedented chemistry performed on acetyl-CoA.
UR - http://www.scopus.com/inward/record.url?scp=84922060886&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84922060886&partnerID=8YFLogxK
U2 - 10.1038/nchembio.1610
DO - 10.1038/nchembio.1610
M3 - Article
C2 - 25151136
AN - SCOPUS:84922060886
SN - 1552-4450
VL - 10
SP - 810
EP - 812
JO - Nature chemical biology
JF - Nature chemical biology
IS - 10
ER -