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Structural evidence for product stabilization by the ribosomal mRNA helicase
Hossein Amiri1, Harry F Noller2
1Center for Molecular Biology of RNA and Department of Molecular, Cell and Developmental Biology, University of California at Santa Cruz, Santa Cruz, California 95064, USA.
RNA (New York, N.Y.)
|December 16, 2018
Summary
The ribosome unwinds messenger RNA (mRNA) structures during protein synthesis. A crystal structure reveals ribosomal protein uS3 may stabilize single-stranded mRNA, aiding this unwinding process.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Protein synthesis involves ribosome translocation along messenger RNA (mRNA).
- Ribosomes possess helicase activity to unwind mRNA structures encountered during translocation.
- The precise mechanism of mRNA unwinding and the role of ribosomal proteins uS3, uS4, and uS5 are not fully understood.
Purpose of the Study:
- To elucidate the mechanism of mRNA unwinding by the ribosome.
- To investigate the potential role of ribosomal protein uS3 in the ribosome's helicase activity.
Main Methods:
- X-ray crystallography of the *Escherichia coli* ribosome.
Main Results:
- A crystal structure revealed single-stranded mRNA extending beyond the ribosome's mRNA tunnel entrance.
- This mRNA interacted with a positively charged region on ribosomal protein uS3.
- The binding appeared specific for single-stranded mRNA immediately preceding the tunnel entrance.
Conclusions:
- Ribosomal protein uS3 may contribute to mRNA unwinding through product stabilization.
- This interaction suggests a mechanism for how the ribosome helicase unwinds structured mRNA.
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