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Ribosomal Initiation Complex-Driven Changes in the Stability and Dynamics of Initiation Factor 2 Regulate the Fidelity of Translation Initiation by Jiangning Wang; Kelvin Caban; Ruben L. Gonzalez is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Ribosomal Initiation Complex-Driven Changes in the Stability and Dynamics of Initiation Factor 2 Regulate the Fidelity of Translation Initiation about?

Joining of the large, 50S, ribosomal subunit to the small, 30S, ribosomal subunit initiation complex (IC) during bacterial translation initiation is catalyzed by the initiation factor (IF) IF2. Because the rate of subunit joining is coupled to the IF, transfer RNA (tRNA), and mRNA codon compositions of the 30S IC, the subunit joining reaction functions as a kinetic checkpoint that regulates the fidelity of translation initiation. Recent structural studies suggest that the conformational dynamics of the IF2·tRNA sub-complex forming on the intersubunit surface of the 30S IC may play a significant role in the mechanisms that couple the rate of subunit joining to the IF, tRNA, and codon compositions of the 30S IC. To test this hypothesis, we have developed a single-molecule fluorescence resonance energy transfer signal between IF2 and tRNA that has enabled us to monitor the conformational dynamics of the IF2·tRNA sub-complex across a series of 30S ICs. Our results demonstrate that 30S ICs undergoing rapid subunit joining display a high affinity for IF2 and an IF2·tRNA sub-complex that primarily samples a single conformation. In contrast, 30S ICs that undergo slower subunit joining exhi

Who reads Ribosomal Initiation Complex-Driven Changes in the Stability and Dynamics of Initiation Factor 2 Regulate the Fidelity of Translation Initiation?

Author

Jiangning Wang; Kelvin Caban; Ruben L. Gonzalez

Published

2015

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)