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Polypeptide sequences essential for RNA recognition by an enzyme.

L Regan, J Bowie, P Schimmel

    Science (New York, N.Y.)
    |March 27, 1987
    PubMed
    Summary
    This summary is machine-generated.

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    Researchers identified a small 17-amino acid segment in alanine tRNA synthetase crucial for binding alanine transfer RNA (tRNA). This finding advances understanding of specific RNA-protein interactions.

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Structural Biology

    Background:

    • Complex RNAs, like transfer RNAs (tRNAs), possess intricate secondary and tertiary structures.
    • Protein recognition of RNA structures, particularly tRNA by aminoacyl tRNA synthetases, is not well understood.
    • Evidence suggests dispersed structural elements in tRNA are vital for aminoacyl tRNA synthetase recognition.

    Purpose of the Study:

    • To investigate the specific RNA-binding regions within alanine tRNA synthetase.
    • To identify the key amino acid sequences responsible for alanine-specific tRNA recognition.

    Main Methods:

    • In vitro manipulation of the cloned alaS gene to create alanine tRNA synthetase fragments.
    • Examination of fragment interactions with alanine-specific tRNA.

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    Main Results:

    • Essential recognition sequences were localized to the middle of the polypeptide, near the aminoacyl adenylate synthesis domain.
    • A sequence of fewer than 100 amino acids determined most of the tRNA interaction strength and specificity.
    • A compact 17-amino acid segment accounted for at least 25% of the synthetase-tRNA binding energy.

    Conclusions:

    • Specific RNA recognition by aminoacyl tRNA synthetases may involve a relatively short polypeptide segment.
    • This short segment, when properly folded, is critical for high-affinity tRNA binding.
    • The findings provide insights into the structural basis of RNA-protein interactions in biological systems.