Abstract
K+-depleted 60S ribosomal subunits from rat liver were submitted to a mild treatment with ribonuclease T1. Ribonucleoprotein fragments could be separated on sucrose gradients only when the digested subunits were partially deproteinized with a high KCl concentration (0.6 M) which removed seven proteins more or less completely and 5S RNA. The RNA and protein content of each fragment has been characterized. The largest ribonucleoprotein enclosed two RNA fragments of about 950,000 and 750,000 daltons and all the salt-resistant proteins except L5. The smallest one enclosed protein L5 (with L11, L17 and L26 in small amounts) and a 67,000 RNA piece. The subsequent hydrolysis of the large ribonucleoprotein produced several other ribonucleoproteins. One of them has been fully characterized: it enclosed a 250,000 RNA fragment and protein L12 (with L11, L25 and L30 in smaller amounts).
Full text
PDF
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Marion M. J., Marion C., Arpin M., Reboud A. M., Reboud J. P. Effect of ribonuclease T1 on ribosomal subunits of rat liver. Nucleic Acids Res. 1976 Oct;3(10):2563–2573. doi: 10.1093/nar/3.10.2563. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Metspalu A., Saarma M., Villems R., Ustav M., Lind A. Interaction of 5-S RNA, 5.8-S RNA and tRNA with rat-liver ribosomal proteins. Eur J Biochem. 1978 Nov 2;91(1):73–81. doi: 10.1111/j.1432-1033.1978.tb20938.x. [DOI] [PubMed] [Google Scholar]
- Metspalu A., Toots I., Saarma M., Villems R. The ternary complex consisting of rat liver ribosomal 5 S RNA, 5.8 S RNA and protein L5. FEBS Lett. 1980 Sep 22;119(1):81–84. doi: 10.1016/0014-5793(80)81002-7. [DOI] [PubMed] [Google Scholar]
- Ulbrich N., Lin A., Wool I. G. Identification by affinity chromatography of the eukaryotic ribosomal proteins that bind to 5.8 S ribosomal ribonucleic acid. J Biol Chem. 1979 Sep 10;254(17):8641–8645. [PubMed] [Google Scholar]
- Ulbrich N., Wool I. G. Identification by affinity chromatography of the eukaryotic ribosomal proteins that bind to 5 S ribosomal ribonucleic acid. J Biol Chem. 1978 Dec 25;253(24):9049–9052. [PubMed] [Google Scholar]