Proton Leakage Is Sensed by IM30 and Activates IM30-Triggered Membrane Fusion

Carmen Siebenaller1, Benedikt Junglas1, Annika Lehmann1

  • 1Department of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.

Insights

Inner membrane protein IM30 stabilizes thylakoid membranes and aids fusion. Acidic conditions enhance IM30

Area of Science:

  • Plant Biology
  • Cell Biology
  • Biochemistry

Background:

  • Inner membrane-associated protein of 30 kDa (IM30) is vital for thylakoid membrane systems in chloroplasts and cyanobacteria.
  • IM30's functions include thylakoid membrane stabilization and Mg2+-dependent membrane fusion, though its precise role is debated.
  • IM30 binds to negatively charged lipids, particularly in stressed membrane areas with proton leakage.

Purpose of the Study:

  • To investigate the effect of acidic environments on IM30's membrane binding and fusion activities.
  • To elucidate the structural changes in IM30 associated with altered activity in acidic conditions.
  • To propose a mechanism for IM30's role in sensing and sealing proton leakage in thylakoid membranes.

Main Methods:

  • In vitro assays to measure IM30's membrane binding.
  • In vitro assays to assess IM30's membrane fusion capabilities.
  • Analysis of protein structural rearrangements in response to pH changes.

Main Results:

  • IM30's membrane binding affinity significantly increases in acidic environments.
  • IM30-mediated membrane fusion activity is markedly enhanced under acidic conditions.
  • Acidic conditions induce structural rearrangements within the IM30 protein.

Conclusions:

  • IM30 exhibits enhanced membrane association and fusion activity in acidic conditions due to structural changes.
  • This acid-induced transition suggests IM30 acts as a sensor for proton leakage at thylakoid membranes.
  • IM30 likely seals compromised membrane regions through fusion, maintaining cellular integrity.

Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
12.1K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
16.3K
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,...
11.5K
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...
4.1K
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...
4.6K
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
13.9K