Affinity labeling of ribosomes.

摘要: Publisher Summary Affinity-labeling studies on the ribosome have as their common goal identification of components functionally important ligand-binding sites. By one generally means individual ribosomal proteins or limited regions rRNA, although occasionally identifications been made at peptide amino acid level, oligonucleotide base level. The ligands whose binding sites explored by affinity labeling include peptidyl-, aminoacyl-, and uncharged tRNA, oligo- polyribonucleotides directed to mRNA-binding locus, protein factors involved in initiation, elongation, translocation, a large number antibiotics. Both photolabile electrophile derivatives used affinity-labeling experiments ribosomes. relative merits these approaches considered detail elsewhere. In addition, covalent incorporation into ribosomes has induced direct sensitized photolysis ligand complexes, well treatment such complexes with bifunctional cross-linking reagents. Reagents employed that contain two electrophilic centers, center, or, case psoralen, centers.