Genetic evidence against the 16S ribosomal RNA helix 27 conformational switch model.

ABSTRACT: A mechanistic understanding of ribosome function demands knowledge of the conformational changes that occur during protein synthesis. One current model proposes a conformational switch in Helix 27 (H27) of 16S rRNA involved in the decoding of mRNA. This model was based on the behavior of mutations in the 912 region of H27 of Escherichia coli 16S rRNA, which were predicted to stabilize the helix in either of two alternative conformations. This interpretation was supported by evidence from both genetics and structural biochemistry. However, recently published X-ray crystallographic structures of the Thermus thermophilus 30S subunit at different stages of tRNA selection have raised doubts regarding the validity of this model. We have therefore revisited the model genetically by constructing a

SUBMITTER: Rodriguez-Correa D 

PROVIDER: S-EPMC1370515 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature