The bacterial toxin RelE induces specific mRNA cleavage in the A site of the eukaryote ribosome.
RelE/RelB is a well-characterized toxin-anti-toxin pair involved in nutritional stress responses in Bacteria and Archae. RelE lacks any eukaryote homolog, but we demonstrate here that it efficiently and specifically cleaves mRNA in the A site of the eukaryote ribosome. The cleavage mechanism is similar to that in bacteria, showing the feasibility of A-site cleavage of mRNA for regulatory purposes also in eukaryotes. RelE cleavage in the A-site codon of a stalled eukaryote ribosome is precise and easily monitored, making "RelE printing" a useful complement to toeprinting to determine the exact mRNA location on the eukaryote ribosome and to probe the occupancy of its A site.
Andreev
Dmitri
D
Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.
Hauryliuk
Vasili
V
Terenin
Ilya
I
Dmitriev
Sergey
S
Ehrenberg
Måns
M
Shatsky
Ivan
I
D000818:Animals; D001427:Bacterial Toxins / Q000737:chemistry*; D001483:Base Sequence; D029968:Escherichia coli Proteins / Q000737:chemistry*; D005821:Genetic Techniques; D016174:Hepacivirus / Q000235:genetics; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000737:chemistry*; D012343:RNA, Transfer / Q000737:chemistry; D012367:RNA, Viral / Q000737:chemistry; D011817:Rabbits; D012156:Reticulocytes / Q000737:chemistry; D012270:Ribosomes / Q000737:chemistry*
D001427:Bacterial Toxins; D029968:Escherichia coli Proteins; D012333:RNA, Messenger; D012367:RNA, Viral; C465566:RelE protein, E coli; D012343:RNA, Transfer