MOM19, an import receptor for mitochondrial precursor proteins

T Söllner1, G Griffiths, R Pfaller

  • 1Institut für Physiologische Chemie, Universität München, Federal Republic of Germany.

Cell
|December 22, 1989
PubMed

Insights

Researchers identified MOM19, a mitochondrial outer membrane protein. Antibodies against MOM19 block the import of many precursor proteins into mitochondria, suggesting MOM19 is a key import receptor.

Area of Science:

  • Mitochondrial biology
  • Protein import
  • Cellular and molecular biology

Background:

  • Mitochondria import numerous proteins to carry out their functions.
  • The mechanisms and specific receptors involved in mitochondrial protein import are not fully elucidated.
  • Previous studies suggested distinct import pathways for different mitochondrial proteins.

Purpose of the Study:

  • To identify and characterize proteins involved in the mitochondrial protein import process.
  • To investigate the role of a newly identified 19 kd protein of the mitochondrial outer membrane (MOM19) in protein import.
  • To determine if MOM19 functions as a specific mitochondrial import receptor.

Main Methods:

  • Identification of a 19 kd protein in the mitochondrial outer membrane (MOM19).
  • Utilized monospecific IgG and Fab fragments against MOM19.
  • Assessed the effect of these antibodies on the import of various precursor proteins into mitochondria.
  • Analyzed the binding affinity of precursors to mitochondria.

Main Results:

  • Monospecific antibodies against MOM19 inhibited the import of precursor proteins for multiple mitochondrial subcompartments.
  • Inhibition occurred at the stage of high-affinity precursor binding to the mitochondria.
  • Import of ADP/ATP carrier and cytochrome c precursors was not inhibited, aligning with distinct import site hypotheses.
  • MOM19 is implicated in the import pathway for a subset of mitochondrial proteins.

Conclusions:

  • MOM19 is a critical component of the mitochondrial protein import machinery.
  • MOM19 functions as, or is closely associated with, a specific receptor for mitochondrial import.
  • The findings support the existence of distinct import pathways mediated by specific receptors like MOM19.

Related Concept Videos

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...
4.4K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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...
2.9K
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,...
8.8K
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...
4.6K
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...
3.5K
Structure of Porins01:21

Structure of Porins

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