Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme

ABSTRACT Membrane deformation by proteins is a universal phenomenon that has been studied extensively in eukaryotes but much less in prokaryotes. In this study, we discovered a membrane-deforming activity of the phospholipid N-methyltransferase PmtA from the plant-pathogenic bacterium Agrobacterium...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Linna Danne, Meriyem Aktas, Andreas Unger, Wolfgang A. Linke, Ralf Erdmann, Franz Narberhaus
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2017
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/38f61ef5565d4fa48b189ccb09fbe576
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:38f61ef5565d4fa48b189ccb09fbe576
record_format	dspace
spelling	oai:doaj.org-article:38f61ef5565d4fa48b189ccb09fbe5762021-11-15T15:51:06ZMembrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme10.1128/mBio.02082-162150-7511https://doaj.org/article/38f61ef5565d4fa48b189ccb09fbe5762017-03-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.02082-16https://doaj.org/toc/2150-7511ABSTRACT Membrane deformation by proteins is a universal phenomenon that has been studied extensively in eukaryotes but much less in prokaryotes. In this study, we discovered a membrane-deforming activity of the phospholipid N-methyltransferase PmtA from the plant-pathogenic bacterium Agrobacterium tumefaciens. PmtA catalyzes the successive three-step N-methylation of phosphatidylethanolamine to phosphatidylcholine. Here, we defined the lipid and protein requirements for the membrane-remodeling activity of PmtA by a combination of transmission electron microscopy and liposome interaction studies. Dependent on the lipid composition, PmtA changes the shape of spherical liposomes either into filaments or small vesicles. Upon overproduction of PmtA in A. tumefaciens, vesicle-like structures occur in the cytoplasm, dependent on the presence of the anionic lipid cardiolipin. The N-terminal lipid-binding α-helix (αA) is involved in membrane deformation by PmtA. Two functionally distinct and spatially separated regions in αA can be distinguished. Anionic interactions by positively charged amino acids on one face of the helix are responsible for membrane recruitment of the enzyme. The opposite hydrophobic face of the helix is required for membrane remodeling, presumably by shallow insertion into the lipid bilayer. IMPORTANCE The ability to alter the morphology of biological membranes is known for a small number of some bacterial proteins. Our study adds the phospholipid N-methyltransferase PmtA as a new member to the category of bacterial membrane-remodeling proteins. A combination of in vivo and in vitro methods reveals the molecular requirements for membrane deformation at the protein and phospholipid level. The dual functionality of PmtA suggests a contribution of membrane biosynthesis enzymes to the complex morphology of bacterial membranes.Linna DanneMeriyem AktasAndreas UngerWolfgang A. LinkeRalf ErdmannFranz NarberhausAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 8, Iss 1 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Linna Danne Meriyem Aktas Andreas Unger Wolfgang A. Linke Ralf Erdmann Franz Narberhaus Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme
description	ABSTRACT Membrane deformation by proteins is a universal phenomenon that has been studied extensively in eukaryotes but much less in prokaryotes. In this study, we discovered a membrane-deforming activity of the phospholipid N-methyltransferase PmtA from the plant-pathogenic bacterium Agrobacterium tumefaciens. PmtA catalyzes the successive three-step N-methylation of phosphatidylethanolamine to phosphatidylcholine. Here, we defined the lipid and protein requirements for the membrane-remodeling activity of PmtA by a combination of transmission electron microscopy and liposome interaction studies. Dependent on the lipid composition, PmtA changes the shape of spherical liposomes either into filaments or small vesicles. Upon overproduction of PmtA in A. tumefaciens, vesicle-like structures occur in the cytoplasm, dependent on the presence of the anionic lipid cardiolipin. The N-terminal lipid-binding α-helix (αA) is involved in membrane deformation by PmtA. Two functionally distinct and spatially separated regions in αA can be distinguished. Anionic interactions by positively charged amino acids on one face of the helix are responsible for membrane recruitment of the enzyme. The opposite hydrophobic face of the helix is required for membrane remodeling, presumably by shallow insertion into the lipid bilayer. IMPORTANCE The ability to alter the morphology of biological membranes is known for a small number of some bacterial proteins. Our study adds the phospholipid N-methyltransferase PmtA as a new member to the category of bacterial membrane-remodeling proteins. A combination of in vivo and in vitro methods reveals the molecular requirements for membrane deformation at the protein and phospholipid level. The dual functionality of PmtA suggests a contribution of membrane biosynthesis enzymes to the complex morphology of bacterial membranes.
format	article
author	Linna Danne Meriyem Aktas Andreas Unger Wolfgang A. Linke Ralf Erdmann Franz Narberhaus
author_facet	Linna Danne Meriyem Aktas Andreas Unger Wolfgang A. Linke Ralf Erdmann Franz Narberhaus
author_sort	Linna Danne
title	Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme
title_short	Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme
title_full	Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme
title_fullStr	Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme
title_full_unstemmed	Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme
title_sort	membrane remodeling by a bacterial phospholipid-methylating enzyme
publisher	American Society for Microbiology
publishDate	2017
url	https://doaj.org/article/38f61ef5565d4fa48b189ccb09fbe576
work_keys_str_mv	AT linnadanne membraneremodelingbyabacterialphospholipidmethylatingenzyme AT meriyemaktas membraneremodelingbyabacterialphospholipidmethylatingenzyme AT andreasunger membraneremodelingbyabacterialphospholipidmethylatingenzyme AT wolfgangalinke membraneremodelingbyabacterialphospholipidmethylatingenzyme AT ralferdmann membraneremodelingbyabacterialphospholipidmethylatingenzyme AT franznarberhaus membraneremodelingbyabacterialphospholipidmethylatingenzyme
_version_	1718427390759141376

Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme

Ejemplares similares