Hryc 2023 Nat Commun: Difference between revisions
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|title=Hryc CF, Mallampalli VKPS, Bovshik EI, Azinas S, Fan G, Serysheva II, Sparagna GC, Baker ML, Mileykovskaya E, Dowhan W (2023) Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex. https://doi.org/10.1038/s41467-023-38441-5 | |title=Hryc CF, Mallampalli VKPS, Bovshik EI, Azinas S, Fan G, Serysheva II, Sparagna GC, Baker ML, Mileykovskaya E, Dowhan W (2023) Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex. https://doi.org/10.1038/s41467-023-38441-5 | ||
|info=Nat Commun 14:2783. [https://pubmed.ncbi.nlm.nih.gov/37188665 PMID: 37188665 Open Access] | |info=Nat Commun 14:2783. [https://pubmed.ncbi.nlm.nih.gov/37188665 PMID: 37188665 Open Access] | ||
|authors=Hryc | |authors=Hryc Corey F, Mallampalli Venkata KPS, Bovshik Evgeniy I, Azinas Stavros, Fan Guizhen, Serysheva Irina I, Sparagna Genevieve C, Baker Matthew L, Mileykovskaya Eugenia, Dowhan William | ||
|year=2023 | |year=2023 | ||
|journal=Nat Commun | |journal=Nat Commun | ||
|abstract=Cardiolipin is a hallmark phospholipid of mitochondrial membranes. Despite established significance of cardiolipin in supporting respiratory supercomplex organization, a mechanistic understanding of this lipid-protein interaction is still lacking. To address the essential role of cardiolipin in supercomplex organization, we report cryo-EM structures of a wild type supercomplex ( | |abstract=Cardiolipin is a hallmark phospholipid of mitochondrial membranes. Despite established significance of cardiolipin in supporting respiratory supercomplex organization, a mechanistic understanding of this lipid-protein interaction is still lacking. To address the essential role of cardiolipin in supercomplex organization, we report cryo-EM structures of a wild type supercomplex (IV<sub>1</sub>III<sub>2</sub>IV<sub>1</sub>) and a supercomplex (III<sub>2</sub>IV<sub>1</sub>) isolated from a cardiolipin-lacking ''Saccharomyces cerevisiae'' mutant at 3.2-Å and 3.3-Å resolution, respectively, and demonstrate that phosphatidylglycerol in III<sub>2</sub>IV<sub>1</sub> occupies similar positions as cardiolipin in IV<sub>1</sub>III<sub>2</sub>IV<sub>1</sub>. Lipid-protein interactions within these complexes differ, which conceivably underlies the reduced level of IV<sub>1</sub>III<sub>2</sub>IV<sub>1</sub> and high levels of III<sub>2</sub>IV<sub>1</sub> and free III<sub>2</sub> and IV in mutant mitochondria. Here we show that anionic phospholipids interact with positive amino acids and appear to nucleate a phospholipid domain at the interface between the individual complexes, which dampen charge repulsion and further stabilize interaction, respectively, between individual complexes. | ||
|editor=[[Plangger M]] | |editor=[[Plangger M]] | ||
|mipnetlab=US CO Aurora Sparagna GC | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration | |area=Respiration, mt-Membrane | ||
|organism=Saccharomyces cerevisiae | |||
|preparations=Isolated mitochondria | |||
|enzymes=Supercomplex | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|additional=2023-06 | |additional=2023-06 | ||
}} | }} | ||
Latest revision as of 15:02, 7 June 2023
| Hryc CF, Mallampalli VKPS, Bovshik EI, Azinas S, Fan G, Serysheva II, Sparagna GC, Baker ML, Mileykovskaya E, Dowhan W (2023) Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex. https://doi.org/10.1038/s41467-023-38441-5 |
» Nat Commun 14:2783. PMID: 37188665 Open Access
Hryc Corey F, Mallampalli Venkata KPS, Bovshik Evgeniy I, Azinas Stavros, Fan Guizhen, Serysheva Irina I, Sparagna Genevieve C, Baker Matthew L, Mileykovskaya Eugenia, Dowhan William (2023) Nat Commun
Abstract: Cardiolipin is a hallmark phospholipid of mitochondrial membranes. Despite established significance of cardiolipin in supporting respiratory supercomplex organization, a mechanistic understanding of this lipid-protein interaction is still lacking. To address the essential role of cardiolipin in supercomplex organization, we report cryo-EM structures of a wild type supercomplex (IV1III2IV1) and a supercomplex (III2IV1) isolated from a cardiolipin-lacking Saccharomyces cerevisiae mutant at 3.2-Å and 3.3-Å resolution, respectively, and demonstrate that phosphatidylglycerol in III2IV1 occupies similar positions as cardiolipin in IV1III2IV1. Lipid-protein interactions within these complexes differ, which conceivably underlies the reduced level of IV1III2IV1 and high levels of III2IV1 and free III2 and IV in mutant mitochondria. Here we show that anionic phospholipids interact with positive amino acids and appear to nucleate a phospholipid domain at the interface between the individual complexes, which dampen charge repulsion and further stabilize interaction, respectively, between individual complexes.
• Bioblast editor: Plangger M • O2k-Network Lab: US CO Aurora Sparagna GC
Labels: MiParea: Respiration, mt-Membrane
Organism: Saccharomyces cerevisiae
Preparation: Isolated mitochondria Enzyme: Supercomplex
HRR: Oxygraph-2k
2023-06
