Dynamic structure of the sarcin/ricin domain in rat 28S ribosomal RNA investigated by hybridization with oligodeoxynucleotide.
In the static state of the ribosome, its S/R domain is not accessible to a probe of 1 4-mer oligodeoxyribonucleotide complementary to the region. However, during the in vitro translation process, the probe can specifically hybridize with the region in ribosome and inhibit translation. It appears that the S/R domain is well-protected when the ribosome is in the static state. This site is partially exposed at some stage(s) of translation. These results indicate that the S/R domain is not a simple single-strand, but a reversibly dynamic structure.
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Shanghai Institute of Biochemistry, Academia Sinica, China.
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D000818:Animals; D002021:Buffers; D002474:Cell-Free System; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism*; D005656:Fungal Proteins; D008099:Liver / Q000737:chemistry; D009693:Nucleic Acid Hybridization; D015345:Oligonucleotide Probes / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011500:Protein Synthesis Inhibitors / Q000737:chemistry / Q000378:metabolism; D012339:RNA, Ribosomal, 28S / Q000737:chemistry* / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012276:Ricin / Q000737:chemistry* / Q000378:metabolism*; D014158:Transcription, Genetic
D002021:Buffers; D005656:Fungal Proteins; D015345:Oligonucleotide Probes; D011500:Protein Synthesis Inhibitors; D012339:RNA, Ribosomal, 28S; C014801:alpha-sarcin; D012276:Ricin; D004722:Endoribonucleases