Mitochondrial porin VDAC 1 seems to be functional in rickettsial cells

Victor V Emelyanov1

  • 1Institute of Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom. Victor.Emelyanov@ncl.ac.uk

Insights

Spotted fever group rickettsiae import mitochondrial porin VDAC1, suggesting a functional role within the bacteria. This import may be linked to their obligate endosymbiotic lifestyle.

Area of Science:

  • Microbiology
  • Cell Biology
  • Evolutionary Biology

Background:

  • Rickettsia prowazekii, a typhus group rickettsia, has been shown to incorporate human mitochondrial porin VDAC1.
  • Porins are crucial protein channels in mitochondrial outer membranes.

Purpose of the Study:

  • To investigate the import of porin by spotted fever group rickettsiae.
  • To explore the localization and potential function of imported porin within rickettsial cells.
  • To propose an evolutionary scenario for the origin of protein import machinery in Rickettsiales.

Main Methods:

  • Differential ultracentrifugation of Rickettsia canadensis cells in Renografin density gradients.
  • Fractionation of total membranes via linear sucrose density gradients after French-press lysis.
  • Analysis of VDAC1 content in different rickettsial membrane fractions.

Main Results:

  • Rickettsial cells from the heavy band (permeabilized) contained significantly more VDAC1 than cells from the light band (non-permeabilized).
  • Outer rickettsial membranes lacked porin, while an intermediate density fraction, likely representing Bayer's adhesion zones, was enriched in VDAC1.
  • Imported porin appears to localize to contact sites between the inner and outer rickettsial membranes.

Conclusions:

  • Mitochondrial porin VDAC1 is imported by spotted fever group rickettsiae, hinting at a functional role.
  • The localization of VDAC1 to contact sites suggests involvement in inter-membrane interactions.
  • The findings support an evolutionary link between Rickettsiales and mitochondria, potentially explaining their obligate endosymbiotic nature.

Related Concept Videos

Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a virus that...
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...
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...
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...
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,...
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...