Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

3.3K
3.3K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

3.1K
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...
3.1K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.2K
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,...
3.2K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

4.4K
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...
4.4K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.6K
Structure of Porins01:21

Structure of Porins

3.0K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Folding the message: mRNA structure as a regulatory layer of human mitochondrial gene expression.

Biochimica et biophysica acta. Molecular cell research·2026
Same author

When membrane insertion sets the pace of mitochondrial translation.

Nature structural & molecular biology·2026
Same author

Structural basis of TACO1-mediated efficient mitochondrial translation.

Nature communications·2026
Same author

Intra-procedure white blood cell monitoring as a predictor of collection efficiency in mononuclear cell apheresis.

Transfusion and apheresis science : official journal of the World Apheresis Association : official journal of the European Society for Haemapheresis·2026
Same author

Structural basis for late maturation steps of mitochondrial respiratory chain complex IV within the human respirasome.

Nature communications·2026
Same author

Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.

bioRxiv : the preprint server for biology·2025
Same journal

Isolation of Mesenchymal Stem Cell-Derived Extracellular Vesicles.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Modeling Melanoma Immune Surveillance by CAR-T Cells in Human Skin Organoids.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Stepwise Optimization of a Matrigel-Based In Vitro Angiogenesis Assay for Reproducible and Quantifiable 2D-Tube Formation Using HUVECs.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Quantifying Mechanical Properties of Fresh Ovarian Tissue with Optical Brillouin Microscopy.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

3D Chromatin Architecture During Early Development: New Methods and New Findings.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Metabolic Plasticity in Embryogenesis Throughout the Lens of NAD<sup></sup>.

Methods in molecular biology (Clifton, N.J.)·2026
See all related articles

Related Experiment Video

Updated: Jul 30, 2025

Rapid Isolation of the Mitoribosome from HEK Cells
09:33

Rapid Isolation of the Mitoribosome from HEK Cells

Published on: October 4, 2018

11.1K

Mitoribosome Biogenesis.

J Conor Moran1, Samuel Del'Olio2, Austin Choi3

  • 1Department of Biochemistry and Molecular Biology, University of Miami, Miller School of Medicine, Miami, FL, USA.

Methods in Molecular Biology (Clifton, N.J.)
|May 11, 2023
PubMed
Summary
This summary is machine-generated.

Mitoribosome biogenesis is a complex process involving mitochondrial and nuclear genes. Assembly factors coordinate ribosomal RNA processing and protein association, with recent cryo-EM structures aiding understanding.

Keywords:
Mitochondrial diseaseMitochondrial ribosomeMitochondrial translationMitoribosome assemblyOXPHOS deficiency

More Related Videos

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 25, 2011

20.0K
Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale
10:56

Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale

Published on: May 17, 2014

68.7K

Related Experiment Videos

Last Updated: Jul 30, 2025

Rapid Isolation of the Mitoribosome from HEK Cells
09:33

Rapid Isolation of the Mitoribosome from HEK Cells

Published on: October 4, 2018

11.1K
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 25, 2011

20.0K
Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale
10:56

Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale

Published on: May 17, 2014

68.7K

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Mitoribosome biogenesis is essential for cellular respiration.
  • It involves mitochondrial and nuclear genomes, and numerous assembly factors.
  • Understanding this process is crucial for cellular function.

Purpose of the Study:

  • To summarize current knowledge on mammalian mitoribosome biogenesis.
  • To highlight the roles of nucleus-encoded assembly factors.
  • To emphasize biological sources and methodologies used in the field.

Main Methods:

  • Biochemical studies.
  • Cryo-electron microscopy (cryo-EM) of mammalian mitoribosomes.
  • Review of existing literature and research approaches.

Main Results:

  • Mitoribosome assembly is a stepwise, hierarchical process.
  • Nucleus-encoded assembly factors are critical catalysts.
  • Cryo-EM provides high-resolution structural insights into assembly intermediates.

Conclusions:

  • Mammalian mitoribosome biogenesis is a highly coordinated pathway.
  • Further structural and biochemical studies will refine our understanding.
  • This knowledge is vital for comprehending mitochondrial function and disease.