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Updated: Aug 1, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
11:19

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses

Published on: February 26, 2011

80Sリボソームの新生タンパク質の出口チャネルの位置

R A Milligan, P N Unwin

    Nature
    |February 20, 1986
    PubMed
    まとめ

    エンドプラズマ網膜の膜に結晶を形成するリボソームは,新しい構造的詳細を明らかにします. 大型サブユニットの低密度領域は,新生タンパク質のマッピングをします.

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    関連する概念動画

    Termination of Translation01:44

    Termination of Translation

    The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
    Directing Proteins to the Rough Endoplasmic Reticulum01:34

    Directing Proteins to the Rough Endoplasmic Reticulum

    The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
    Cotranslational Protein Translocation01:20

    Cotranslational Protein Translocation

    Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
    Sec61 channel partners for cotranslational translocation
    During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
    Insertion of Single-pass Transmembrane Proteins in the RER01:26

    Insertion of Single-pass Transmembrane Proteins in the RER

    Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
    Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
    Post-translational Translocation of Proteins to the RER01:27

    Post-translational Translocation of Proteins to the RER

    A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
    Targeting proteins to the ER
    Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
    Ribosomes01:27

    Ribosomes

    Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
    Ribosome Structure and Assembly
    Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within...