The protein import receptor MOM19 of yeast mitochondria

M Moczko1, F Gärtner, N Pfanner

  • 1Biochemisches Institut, Universität Freiburg, Germany.

FEBS Letters
|July 12, 1993
PubMed

Insights

Mitochondrial protein import receptor MOM19 (MOM19) is crucial for yeast mitochondria. This study shows MOM19 functions independently of MOM72 in preprotein translocation across the outer membrane.

Area of Science:

  • Mitochondrial biogenesis
  • Protein translocation
  • Cell biology

Background:

  • Mitochondria import proteins through a complex process involving outer membrane receptors.
  • The roles of specific receptors like MOM19 and MOM72 in yeast mitochondrial protein import are under investigation.

Purpose of the Study:

  • To identify and characterize the protein import receptor MOM19 in Saccharomyces cerevisiae mitochondria.
  • To determine the functional relationship between MOM19 and MOM72 in protein import.

Main Methods:

  • Antibodies and Fab fragments against MOM19 were used to inhibit protein import.
  • Experiments were conducted using wild-type and MOM72-deficient yeast mitochondria.

Main Results:

  • MOM19 was identified as a protein exposed on the outer mitochondrial membrane and part of the receptor complex.
  • Antibodies targeting MOM19 significantly inhibited preprotein import into isolated mitochondria.
  • Preprotein import mediated by MOM19 was not dependent on the presence of the MOM72 receptor.

Conclusions:

  • MOM19 is essential for preprotein translocation across the yeast mitochondrial outer membrane.
  • MOM19 functions independently of the MOM72 receptor in this process.

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...
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 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...
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 precursors...