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Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins
Mirka Kutzner1, Benedikt Junglas2, Mayank Sharma3
1Department of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, Mainz, Germany.
Abstract:
More than three decades ago, the inner membrane-associated protein of 30 kDa (IM30), also known as Vipp1, was identified in pea chloroplasts to bind to the chloroplast inner envelope membrane. IM30/Vipp1 is a membrane-associated and soluble stromal protein and is proposed to mediate vesicle formation. Furthermore, it is linked to membrane stabilization processes, as also discussed for its bacterial homolog PspA. More recently, the structures of cyanobacterial IM30/Vipp1 and PspA proteins were resolved, revealing that these proteins belong to the endosomal sorting complex required for transport III (ESCRT-III) superfamily. ESCRT-IIIs are known for their central roles in diverse membrane remodeling activities in eukaryotic cells. This discovery, together with recent in vitro studies, now enables a molecular understanding of IM30/Vipp1 structure and activity in cyanobacteria and chloroplasts, an organelle of cyanobacterial origin. Here, we discuss membrane binding of IM30/Vipp1 in chloroplasts/cyanobacteria, contrasting them with eukaryotic ESCRT-III function. Recent analyses have identified two key regions in IM30/Vipp1 that mediate initial membrane binding, as well as the formation of spiral, barrel, and/or rod structures on membrane surfaces, eventually facilitating membrane internalizations and tubulation. The potential roles of these membrane-bound structures in the remodeling of chloroplasts and cyanobacterial membranes are discussed.
Insights
Inner membrane protein IM30/Vipp1 binds to chloroplasts and cyanobacteria membranes, mediating vesicle formation and membrane remodeling. Its structure and function are linked to the ESCRT-III superfamily.
Area of Science:
- Cell Biology
- Molecular Biology
- Organelle Biology
Background:
- Inner membrane protein IM30 (Vipp1) identified in pea chloroplasts binds to the inner envelope membrane.
- IM30/Vipp1 is involved in vesicle formation and membrane stabilization, similar to its bacterial homolog PspA.
- IM30/Vipp1 and PspA belong to the ESCRT-III superfamily, known for membrane remodeling in eukaryotes.
Purpose of the Study:
- To provide a molecular understanding of IM30/Vipp1 structure and activity in cyanobacteria and chloroplasts.
- To discuss the membrane binding of IM30/Vipp1 in chloroplasts/cyanobacteria and contrast it with eukaryotic ESCRT-III function.
- To explore the roles of IM30/Vipp1 in membrane remodeling, including internalizations and tubulation.
Main Methods:
- Structural resolution of cyanobacterial IM30/Vipp1 and PspA proteins.
- In vitro studies to understand IM30/Vipp1 structure and activity.
- Analysis of key regions in IM30/Vipp1 mediating membrane binding and structure formation.
Main Results:
- IM30/Vipp1 binds to chloroplast and cyanobacterial membranes.
- Two key regions in IM30/Vipp1 mediate initial membrane binding.
- IM30/Vipp1 forms spiral, barrel, and/or rod structures on membrane surfaces, facilitating internalizations and tubulation.
Conclusions:
- IM30/Vipp1 plays a crucial role in membrane remodeling in chloroplasts and cyanobacteria.
- The ESCRT-III superfamily's function in membrane remodeling extends to chloroplasts and cyanobacteria.
- Understanding IM30/Vipp1 structure and function offers insights into organelle biogenesis and membrane dynamics.
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