PMID:16246364
| Citation |
Holmes, KL and Culver, GM (2005) Analysis of conformational changes in 16 S rRNA during the course of 30 S subunit assembly. J. Mol. Biol. 354:340-57 |
|---|---|
| Abstract |
Ribosome biogenesis involves an integrated series of binding events coupled with conformational changes that ultimately result in the formation of a functional macromolecular complex. In vitro, Escherichia coli 30 S subunit assembly occurs in a cooperative manner with the ordered addition of 20 ribosomal proteins (r-proteins) with 16 S rRNA. The assembly pathway for 30 S subunits has been dissected in vitro into three steps, where specific r-proteins associate with 16 S rRNA early in 30 S subunit assembly, followed by a mid-assembly conformational rearrangement of the complex that then enables the remaining r-proteins to associate in the final step. Although the three steps of 30 S subunit assembly have been known for some time, few details have been elucidated about changes that occur as a result of these three specific stages. Here, we present a detailed analysis of the concerted early and late stages of small ribosomal subunit assembly. Conformational changes, roles for base-pairing and r-proteins at specific stages of assembly, and a polar nature to the assembly process have been revealed. This work has allowed a more comprehensive and global view of E.coli 30 S ribosomal subunit assembly to be obtained. |
| Links |
PubMed Online version:10.1016/j.jmb.2005.09.056 |
| Keywords |
Base Pairing; Escherichia coli/chemistry; Escherichia coli/genetics; Models, Molecular; Nucleic Acid Conformation; Protein Subunits; RNA, Bacterial/chemistry; RNA, Bacterial/genetics; RNA, Ribosomal, 16S/chemistry; RNA, Ribosomal, 16S/metabolism; Ribosomal Proteins/chemistry; Ribosomal Proteins/genetics; Ribosomal Proteins/metabolism; Ribosomes/chemistry; Ribosomes/metabolism |
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