RALyase; a terminator of elongation function of depurinated ribosomes.
Plant ribosomal RNA apurinic site specific lyase (RALyase) cleaves the phosphodiester bond at the depurinated site produced by ribosome-inactivating protein, while the biological role of this enzyme is not clear. As the depurinated ribosomes retain weak translation elongation activities, it was suggested that RALyase completes the ribosome inactivation. To confirm this point, we measured the effects of the phosphodiester cleavage using a fusion of wheat RALyase produced with a cell-free protein synthesis system from wheat germ. The results indicated that RALyase diminishes the residual elongation activities of the depurinated ribosomes.
Ozawa
Akihiko
A
Department of Applied Chemistry, Faculty of Engineering, Ehime University, Matsuyama, 790-8577, Japan.
Sawasaki
Tatsuya
T
Takai
Kazuyuki
K
Uchiumi
Toshio
T
Hori
Hiroyuki
H
Endo
Yaeta
Y
D000818:Animals; D002474:Cell-Free System; D004722:Endoribonucleases / Q000138:chemical synthesis / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D020652:Peptide Elongation Factor 2 / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000378:metabolism*; D010455:Peptides / Q000138:chemical synthesis; D011072:Poly U / Q000378:metabolism; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology*; D012335:RNA, Ribosomal / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000138:chemical synthesis / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D012270:Ribosomes / Q000378:metabolism*; D013552:Swine; D014908:Triticum
D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D010455:Peptides; D011500:Protein Synthesis Inhibitors; D012335:RNA, Ribosomal; D011993:Recombinant Fusion Proteins; D011072:Poly U; C012001:polyphenylalanine; D004722:Endoribonucleases; C402789:ribosomal RNA apurinic site specific lyase