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    Home > Biochemistry News > Biotechnology News > protein synthesis journey

    protein synthesis journey

    • Last Update: 2022-05-16
    • Source: Internet
    • Author: User
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    The genetic information stored in DNA is "decoded" into proteins through the process of translation
    .
    This involves the formation of peptide bonds between amino acids that bind to transfer RNA (tRNA) molecules that slide in close proximity on the ribosome and elongate the peptide chain, followed by a conformational change to form the protein

    .
    Unlike the codon-dependent recognition of aminoacyl tRNAs in the small ribosomal subunit, the peptide bond formation in question occurs at the peptide transferase center (PTC) of the large ribosomal subunit, in a manner that is not amino acid specific

    .
    This non-specificity suggests that large subunits evolved prior to small subunits, which interact more specifically with mRNAs and tRNAs

    .

    Although the evolution of PTC formation has been thoroughly documented, how ribosomes develop into functional entities and become essential components of protein synthesis is poorly understood
    .
    Scientists have long been puzzled by the fact that tRNAs need the help of a "scaffold" to create a peptide bond that guides them to interact via a 3'-CCA sequence on the receptor arm

    .
    What this scaffold is and how it works will be an interesting research topic

    .

    A team of scientists at Tokyo University of Science, led by Professor Koji Tamura, decided to solve this puzzle with the lens of biological evolutionary continuity
    .
    Their research, published online April 12, 2022 in
    Life , Volume 12, Issue 4, sheds light on the evolutionary aspects of protein translation
    .
    Their findings provide important evidence for the PTC origin and evolution hypothesis, which has changed the way we look at modern ribosomes and tRNAs

    .

    The idea arose after a closer look at the crystal structure of the 70S ribosome-tRNA complex in Thermus thermophilus, a bacterium often used in genetic studies
    .
    Here, the peptidyl (P-) and aminoacyl (A-) sites of the tRNA are aligned, bringing the CCA ends close, like a football player's index finger in "Goromaru pose"

    .
    "There is an entity that acts as a scaffold to maintain this proximity, and it likely originates from primitive PTCs," says Professor Tamura

    .
    As evolutionary aspects are possible, the team chose to use primitive tRNAs, or "small RNA helices," for their studies

    .

    They first attempted to form peptide bonds between two alanine-specific small helices in the presence of fragments of ribosomal RNA
    .
    The peptide bond was formed using the ribosomal fragment P1c2 as an RNA scaffold, which is only 70 nucleotides long! Next, they added a terminal amino acid fragment (sequence UGGU) to P1c2 (P1c2
    UGGU )
    .
    According to the mass spectrometry results, this enables a 4.
    2-fold improvement in peptide bond formation ability! The peptide bond formation between two alanine residues is supported by the dimer
    P1c2
    UGGU
    .
    The UGGU sequence on this scaffold interacts with the corresponding 3' end ACCA on the microhelix, bringing the two amino acids close enough to form a peptide bond

    .
    Nobel laureate Dr.
    Ada Yonath and her team have recently shown that similarly conserved PTC regions can catalyze the formation of peptide bonds in artificially mimicked molecules, but Professor Tamura's team has shown that aminoacylated RNA can also be a substrate

    .

    This finding undoubtedly hints at the possibility that the small helix binds to the original PTC
    .
    So, what do these results suggest about the evolution of the ribosome? "The functional interaction between the CCA and PTC of the tRNA may have been 'corrected' during evolution

    .
    Although current ribosomes do not have contiguous sequences like UGGU, But their interactions are 'conceptually' similar to the effects seen in our study

    .
    It is plausible that small helices eventually evolved into tRNAs, for example, using a kissing loop interaction between two small helix-like RNA molecules," Professor Tamura explained

    .
    "These mini-helix-like molecules, which form part of the peptide bond-forming scaffold, may have contributed not only to the evolution of current PTCs, but also to tRNA molecules," he added

    .

    Future applications of this research -- opening exciting avenues for evolutionary RNA biology -- are manifold
    .
    Faced with a metabolic paradox (the building blocks of DNA and RNA are produced from amino acids), it is conceivable to study the concept of "peptide nucleic acids" as precursors of genetic material

    .
    These results are fascinating, and they will help scientists decipher molecular phenomena that have remained unsolved for years

    .

    Mai Kawabata, Kentaro Kawashima, Hiromi Mutsuro-Aoki, Tadashi Ando, ​​Takuya Umehara, Koji Tamura.
    Peptide Bond Formation between Aminoacyl-Minihelices by a Scaffold Derived from the Peptidyl Transferase Center .
    Life , 2022; 12 (4): 573



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