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Shape-selective RNA recognition by cysteinyl-tRNA synthetase.
Scott Hauenstein1, Chun-Mei Zhang, Ya-Ming Hou
1Department of Chemistry and Biochemistry, University of California at Santa Barbara, Santa Barbara, California 93106-9510, USA.
Nature Structural & Molecular Biology
|October 19, 2004
Summary
The crystal structure of Escherichia coli cysteinyl-tRNA synthetase (CysRS) bound to tRNA(Cys) reveals extensive protein-RNA interactions. This detailed structure explains how CysRS recognizes tRNA(Cys) through specific base and shape interactions.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Cysteinyl-tRNA synthetase (CysRS) is crucial for protein synthesis, attaching cysteine to its cognate tRNA.
- Understanding the CysRS-tRNA(Cys) interaction is key to deciphering aminoacyl-tRNA synthetase function.
Purpose of the Study:
- To elucidate the molecular basis of tRNA recognition by CysRS.
- To determine the high-resolution crystal structure of the CysRS-tRNA(Cys) complex.
Main Methods:
- X-ray crystallography at 2.3 A resolution.
- Mutational analysis of enzyme and tRNA components.
Main Results:
- Revealed extensive, specific interactions between CysRS and tRNA(Cys) at the protein-RNA interface.
- Identified a bent tRNA anticodon stem conformation essential for shape-selective recognition.
- Showcased interactions with the D loop and G15.G48 tertiary base pair, supporting indirect readout mechanisms.
Conclusions:
- The CysRS-tRNA(Cys) complex structure provides atomic-level insights into tRNA aminoacylation specificity.
- Shape-selective recognition and indirect readout mechanisms play significant roles in CysRS function.