Depurination of yeast 26S ribosomal RNA by recombinant ricin A chain.
The nature of the modification of yeast ribosomes by the recombinant form of the ricin A chain has been examined. Evidence is presented that the 26S rRNA molecule is depurinated at a specific site and that the activity is inhibited by antibody raised to ricin A chain. It thus appears that the recombinant form of this toxin retains the depurination activity of the native molecule. These results are consistent with the model that the site of depurination is in a highly conserved sequence forming a loop on the surface of the ribosome, a domain involved in elongation factor-dependent binding of aminoacyl-tRNA.
Bradley
J L
JL
Department of Biochemistry and Molecular Biology, University of Florida, Gainesville 32610.
Silva
H M
HM
McGuire
P M
PM
D011687:Purines / Q000378:metabolism*; D012335:RNA, Ribosomal / Q000378:metabolism*; D011994:Recombinant Proteins / Q000494:pharmacology; D012276:Ricin / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae
D011687:Purines; D012335:RNA, Ribosomal; D011994:Recombinant Proteins; D012276:Ricin