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Delineating the rules for structural adaptation of membrane-associated proteins to evolutionary changes in membrane lipidome
- Source :
- Current Biology, Makarova, M, Peter, M, Balogh, G, Glatz, A, MacRae, J I, Lopez Mora, N, Booth, P, Makeyev, E, Vigh, L & Oliferenko, S 2020, ' Delineating the Rules for Structural Adaptation of Membrane-Associated Proteins to Evolutionary Changes in Membrane Lipidome ', Current Biology, vol. 30, no. 3, pp. 367-380.e8 . https://doi.org/10.1016/j.cub.2019.11.043
- Publication Year :
- 2019
- Publisher :
- Cold Spring Harbor Laboratory, 2019.
-
Abstract
- Summary Membrane function is fundamental to life. Each species explores membrane lipid diversity within a genetically predefined range of possibilities. How membrane lipid composition in turn defines the functional space available for evolution of membrane-centered processes remains largely unknown. We address this fundamental question using related fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. We show that, unlike S. pombe that generates membranes where both glycerophospholipid acyl tails are predominantly 16–18 carbons long, S. japonicus synthesizes unusual “asymmetrical” glycerophospholipids where the tails differ in length by 6–8 carbons. This results in stiffer bilayers with distinct lipid packing properties. Retroengineered S. pombe synthesizing the S.-japonicus-type phospholipids exhibits unfolded protein response and downregulates secretion. Importantly, our protein sequence comparisons and domain swap experiments support the hypothesis that transmembrane helices co-evolve with membranes, suggesting that, on the evolutionary scale, changes in membrane lipid composition may necessitate extensive adaptation of the membrane-associated proteome.<br />Highlights • The two acyl tails in S. japonicus phospholipids tend to differ by 6–8 carbons • S. japonicus but not S. pombe FAS makes both medium and long-chain fatty acids • S. japonicus membranes are more ordered than membranes of its relative S. pombe • Changes in membrane lipids may drive co-evolution of transmembrane helices<br />Makarova et al. show that membranes of related fission yeasts S. pombe and S. japonicus are made of structurally distinct phospholipids because of the difference in fatty acid synthase activities. Bioinformatics and retro-engineering experiments reveal that evolutionary changes in lipid metabolism require adaptation of the membrane-associated proteome.
- Subjects :
- 0301 basic medicine
fission yeasts
adaptation
Protein Structure, Secondary
chemistry.chemical_compound
0302 clinical medicine
Protein sequencing
Ecology,Evolution & Ethology
lipid metabolism
fatty acid synthase
Human Biology & Physiology
0303 health sciences
biology
030302 biochemistry & molecular biology
unfolded protein response
Lipidome
Transmembrane protein
Transmembrane domain
Membrane
membranes
Glycerophospholipid
Proteome
General Agricultural and Biological Sciences
Nuclear Envelope
Immunology
Infectious Disease
Biochemistry & Proteomics
General Biochemistry, Genetics and Molecular Biology
Article
lipids
Evolution, Molecular
Membrane Lipids
Signalling & Oncogenes
03 medical and health sciences
Species Specificity
transmembrane proteins
evolution
Schizosaccharomyces
Computational & Systems Biology
030304 developmental biology
FOS: Clinical medicine
Membrane Proteins
Lipid metabolism
Cell Biology
Tumour Biology
biology.organism_classification
030104 developmental biology
Metabolism
chemistry
Lipidomics
Schizosaccharomyces pombe
Unfolded protein response
Biophysics
Cell Cycle & Chromosomes
030217 neurology & neurosurgery
Developmental Biology
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Current Biology, Makarova, M, Peter, M, Balogh, G, Glatz, A, MacRae, J I, Lopez Mora, N, Booth, P, Makeyev, E, Vigh, L & Oliferenko, S 2020, ' Delineating the Rules for Structural Adaptation of Membrane-Associated Proteins to Evolutionary Changes in Membrane Lipidome ', Current Biology, vol. 30, no. 3, pp. 367-380.e8 . https://doi.org/10.1016/j.cub.2019.11.043
- Accession number :
- edsair.doi.dedup.....036343f7e078a6845192c74d70807b3e
- Full Text :
- https://doi.org/10.1101/762146