A Novel Stress-response Protein That Binds at the Ribosomal Subunit Interface and Arrests Translation (original) (raw)

1. D.E. AGAFONOV,
2. V.A. KOLB, and
3. A.S. SPIRIN
4. Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia 142290

Excerpt

One of the most direct approaches for studies of proteintopography on the ribosome surface is the so-called hottritium bombardment technique (Yusupov and Spirin1988). The technique is based on the replacement of hydrogen by tritium in covalent bonds of macromolecules intheir thin surface layer (Shishkov et al. 1976; Goldanskiiet al. 1988). Studying proteins of the ribosome surfacewith this methodology has led to the finding that anunidentified minor component of Escherichia coli ribosomes corresponding to spot Y on the two-dimensionalelectrophoretic map of ribosomal proteins becomeshighly exposed upon dissociation of the 70S ribosomeinto subunits (Yusupov and Spirin 1986, 1988; Agafonovet al. 1997)...