Abstract
In order to probe the spatial arrangement of proteins within the 5.8 S rRNA domain of the intact ribosomal subunit of Saccharomyces cerevisiae, 60 S ribosomal subunits were treated with 2-iminothiolane. Proteins were extracted from the cross-linked ribosomes, fractionated by Sephadex G-150 column chromatography, and analyzed by diagonal polyacrylamide-sodium dodecyl sulfate gel electrophoresis. Constituent proteins of cross-linked pairs were identified by two-dimensional polyacrylamide gel electrophoresis. Nine cross-links involving five of the 11 5.8 S rRNA-binding proteins were analyzed. A model showing the network of cross-links is presented. Several of the 5.8 S rRNA-binding proteins are in sufficiently close proximity of the ribosomal A-site proteins to be cross-linked.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 9971-9974 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 259 |
| Issue number | 16 |
| Publication status | Published - Jan 1 1984 |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology