title: Probing conformational states of modified helix 69 in 50S ribosomes.
abstract: The movement of the small ribosomal subunit (30S) relative to the large ribosomal subunit (50S) during translation is widely known, but many molecular details and roles of rRNA and proteins in this process are still undefined, especially in solution models. The functional relationship of modified nucleotides to ribosome activity is one such enigma. To better understand ribosome dynamics and the influence of modified nucleotides on such processes, the focus of this work was helix 69 of 23S rRNA, which contains three pseudouridine residues in its loop region. Ribosome probing experiments with dimethylsulfate revealed that specific base accessibilities and individual nucleotide conformations in helix 69 are influenced differently by pH, temperature, magnesium, and the presence of pseudouridine modifications.
authors.affiliation: Department of Chemistry, Wayne State University, Detroit, Michigan 48202, USA.
authors.forename: Yogo
authors.initials: Y
authors.lastname: Sakakibara
authors.forename: Christine S
authors.initials: CS
authors.lastname: Chow
mesh_terms: D020816:Amino Acid Motifs; D004926:Escherichia coli / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008968:Molecular Conformation; D012338:RNA, Ribosomal, 23S / Q000737:chemistry*; D013463:Sulfuric Acid Esters / Q000737:chemistry; D014529:Uridine / Q000737:chemistry
chemical_list: D012338:RNA, Ribosomal, 23S; D013463:Sulfuric Acid Esters; C007482:dimethyl sulfate; D014529:Uridine