Photo-induced protein cross-linking to 5S RNA and 28-5.8S RNA within rat-liver 60S ribosomal subunits.
Rat liver 60S ribosomal subunits were irradiated with 254-nm ultraviolet light (1.26 X 10(4) quanta/subunit), under conditions which preserved their functional activity. Cross-linked RNA-protein complexes were recovered after unreacted proteins had been removed by repeated acetic acid extractions. Proteins linked to the whole rRNA, to 5S RNA and to 28-5.8 S RNAs were identified by two-dimensional gel electrophoresis after RNA hydrolysis by ribonucleases T1 and A. Our results showed that numerous proteins interact with rRNAs (at least ten with 28-5.8 S RNA, eight with 5S RNA and among these three are common to both) and have been discussed in the light of all the available data.
D000818:Animals; D001345:Autoradiography; D004586:Electrophoresis / Q000379:methods; D008099:Liver / Q000378:metabolism / Q000528:radiation effects*; D008970:Molecular Weight; D010777:Photochemistry; D011485:Protein Binding / Q000528:radiation effects; D012335:RNA, Ribosomal / Q000378:metabolism / Q000528:radiation effects*; D051381:Rats; D012269:Ribosomal Proteins / Q000378:metabolism / Q000528:radiation effects*; D012270:Ribosomes / Q000378:metabolism / Q000528:radiation effects*; D014466:Ultraviolet Rays
D012335:RNA, Ribosomal; D012269:Ribosomal Proteins