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Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment techniqueстатья
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 6 февраля 2017 г.
- Авторы: Agafonov D.E., Kolb V.A., Spirin A.S.
- Журнал: Proceedings of the National Academy of Sciences of the United States of America
- Том: 94
- Номер: 24
- Год издания: 1997
- Издательство: National Academy of Sciences
- Местоположение издательства: United States
- Первая страница: 12892
- Последняя страница: 12897
- Аннотация: The hot tritium bombardment technique [Goldanskii, V. I., Kashirin, I. A., Shishkov, A. V., Baratova, L. A. & Grebenshchikov, N. I. (1988) J. Mol. Biol. 201,567-574] has been applied to measure the exposure of proteins on the ribosomal surface. The technique is based on replacement of hydrogen by high energy tritium atoms in thin surface layer of macromolecules. Quantitation of tritium radioactivity of each protein has revealed that proteins S1, S4, S5, S7, S18, S20, and S21 of the small subunit, and proteins L7/L12, L9, L10, L11, L16, L17, L24, and L27 of the large subunit are well exposed on the surface of the Escherichia coli 70 S ribosome. Proteins S8, S10, S12, S16, S17, L14, L20, L29, L30, L31, L32, L33, and L34 have virtually no groups exposed on the ribosomal surface. The remaining proteins are found to be exposed to lesser degree than the well exposed ones. No additional ribosomal proteins was exposed upon dissociation of ribosomes into subunits, thus indicating the absence of proteins on intersubunit contacting surfaces.
- Добавил в систему: Колб Вячеслав Адамович