Cross-linking of L5 protein to 5 S RNA in XXXX liver 60-S subunits by ultraviolet irradiation.

@entity969 @entity3323 @entity35 @entity1098 @entity214
After @entity35 liver 60-S ribosomal subunits were irradiated with ultraviolet light at 254 nm, they were treated with @entity1098 and then subjected to @entity969 density-gradient centrifugation to isolate 5 S RNA-protein complex. When 5 S RNA-protein was analyzed by @entity214 - @entity3323 gel electrophoresis which dissociated noncovalent 5 S RNA-protein, two protein bands were observed. The one showed a slower mobility than the protein band (L5) of 5 S RNA-protein from non-irradiated 60 S subunit and the other showed the same mobility as L5 protein. Since the former band was shown to be specific to ultraviolet-irradiation, it was considered as cross-linked 5 S RNA-protein. After the two protein bands were iodinated with 125 I, labeled protein was extracted and treated with RNAase. Thereafter, it was analyzed by two-dimensional @entity3323 gel electrophoresis, followed by autoradiography. The results indicate that the protein component of cross-linked 5 S RNA-protein is L5 protein (ribosomal protein; these proteins are designated according to the proposed uniform nomenclature. The correlation between that and our nomenclature was reported by McConkey et al. (1979) Mol. Gen. Genet. 169, 1-6. They also confirm the results previously reported (Terao, K., Takahashi, Y. and O(gata, K. (1975) Biochim. Biophys. Acta 402, 230-237).
