RT Journal Article
SR Electronic
T1 Delineating the rules for structural adaptation of membrane-associated proteins to evolutionary changes in membrane lipidome
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 762146
DO 10.1101/762146
A1 Makarova, Maria
A1 Peter, Maria
A1 Balogh, Gabor
A1 Glatz, Attila
A1 MacRae, James I.
A1 Mora, Nestor Lopez
A1 Booth, Paula
A1 Makeyev, Eugene
A1 Vigh, Laszlo
A1 Oliferenko, Snezhana
YR 2019
UL http://biorxiv.org/content/early/2019/09/09/762146.abstract
AB 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 indicate 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.