Related Experiment Video

Updated: Aug 19, 2026

Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation
14:44

Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation

Published on: March 15, 2014

Localization of enzyme for heme attachment to apocytochrome c in yeast mitochondria

S Enosawa, A Ohashi

    Biochemical and Biophysical Research Communications
    |December 30, 1986
    PubMed

    More Related Videos

    Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae08:55

    Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

    Published on: July 19, 2021

    An Improved Method to Isolate Mitochondrial Contact Sites07:55

    An Improved Method to Isolate Mitochondrial Contact Sites

    Published on: June 16, 2023

    Related Concept Videos

    Mitochondrial Membranes01:45

    Mitochondrial Membranes

    A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
    The Inner Mitochondrial Membrane01:28

    The Inner Mitochondrial Membrane

    The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
    Mitochondrial Protein Sorting01:39

    Mitochondrial Protein Sorting

    Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
    Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
    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,...
    Porin Insertion in the Outer Mitochondrial Membrane01:12

    Porin Insertion in the Outer Mitochondrial Membrane

    Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
    Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
    Protein Transport into the Inner Mitochondrial Membrane01:34

    Protein Transport into the Inner Mitochondrial Membrane

    Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
    Transport of mitochondrial precursors across the TIM23 channel is driven by...