関連する実験動画

Updated: Aug 7, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

ATP刺激されたエンドプロテアゼは,E. coliの細胞膜と関連しています

R W Voellmy, A L Goldberg

    Nature
    |April 2, 1981
    PubMed
    まとめ

    バクテリアのタンパク質分解には,タンパク質をペプチドに分解するATP刺激の膜タンパク質酶が含まれます. 溶解性酵素は,これらのペプチドをアミノ酸に完全に水解する.

    さらに関連する動画

    Measuring In Vitro ATPase Activity for Enzymatic Characterization07:38

    Measuring In Vitro ATPase Activity for Enzymatic Characterization

    Published on: August 23, 2016

    Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles13:16

    Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles

    Published on: December 31, 2019

    関連する概念動画

    Translocation of Proteins into the Mitochondria01:19

    Translocation of Proteins into the Mitochondria

    Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
    Sorting of outer membrane proteins:
    Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
    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...
    Tail-anchoring of Proteins in the ER Membrane01:45

    Tail-anchoring of Proteins in the ER Membrane

    Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
    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...
    Protein Translocation Machinery on the ER Membrane01:28

    Protein Translocation Machinery on the ER Membrane

    The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
    Sec61 protein conducting channel
    In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
    The Proteasome Structure01:17

    The Proteasome Structure

    The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
    The proteasome is an...