1. Structural aspects of RbfA action during small ribosomal subunit assembly.
- Author
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Datta PP, Wilson DN, Kawazoe M, Swami NK, Kaminishi T, Sharma MR, Booth TM, Takemoto C, Fucini P, Yokoyama S, and Agrawal RK
- Subjects
- Bacterial Proteins metabolism, Bacterial Proteins physiology, Binding Sites, Cryoelectron Microscopy, Models, Molecular, Protein Structure, Tertiary, RNA, Bacterial metabolism, RNA, Ribosomal, 16S metabolism, RNA-Binding Proteins metabolism, Ribosomal Proteins metabolism, Ribosomal Proteins physiology, Bacterial Proteins chemistry, RNA-Binding Proteins chemistry, Ribosomal Proteins chemistry, Ribosome Subunits, Small, Bacterial metabolism, Thermus thermophilus metabolism
- Abstract
Ribosome binding factor A (RbfA) is a bacterial cold shock response protein, required for an efficient processing of the 5' end of the 16S ribosomal RNA (rRNA) during assembly of the small (30S) ribosomal subunit. Here we present a crystal structure of Thermus thermophilus (Tth) RbfA and a three-dimensional cryo-electron microscopic (EM) map of the Tth 30S*RbfA complex. RbfA binds to the 30S subunit in a position overlapping the binding sites of the A and P site tRNAs, and RbfA's functionally important C terminus extends toward the 5' end of the 16S rRNA. In the presence of RbfA, a portion of the 16S rRNA encompassing helix 44, which is known to be directly involved in mRNA decoding and tRNA binding, is displaced. These results shed light on the role played by RbfA during maturation of the 30S subunit, and also indicate how RbfA provides cells with a translational advantage under conditions of cold shock.
- Published
- 2007
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