@article {2626,
	title = {Membrane-partitioned cell wall synthesis in mycobacteria.},
	journal = {Elife},
	volume = {10},
	year = {2021},
	month = {2021 Feb 05},
	abstract = {<p>Many antibiotics target the assembly of cell wall peptidoglycan, an essential, heteropolymeric mesh that encases most bacteria. In rod-shaped bacteria, cell wall elongation is spatially precise yet relies on limited pools of lipid-linked precursors that generate and are attracted to membrane disorder. By tracking enzymes, substrates, and products of peptidoglycan biosynthesis in , we show that precursors are made in plasma membrane domains that are laterally and biochemically distinct from sites of cell wall assembly. Membrane partitioning likely contributes to robust, orderly peptidoglycan synthesis, suggesting that these domains help template peptidoglycan synthesis. The cell wall-organizing protein DivIVA and the cell wall itself promote domain homeostasis. These data support a model in which the peptidoglycan polymer feeds back on its membrane template to maintain an environment conducive to directional synthesis. Our findings are applicable to rod-shaped bacteria that are phylogenetically distant from , indicating that horizontal compartmentalization of precursors may be a general feature of bacillary cell wall biogenesis.</p>
},
	issn = {2050-084X},
	doi = {10.7554/eLife.60263},
	author = {Garc{\'\i}a-Heredia, Alam and Kado, Takehiro and Sein, Caralyn E and Puffal, Julia and Osman, Sarah H and Judd, Julius and Gray, Todd A and Morita, Yasu S and Siegrist, M Sloan}
}
@article {691,
	title = {Mutations in pimE restore lipoarabinomannan synthesis and growth in a Mycobacterium smegmatis lpqW mutant.},
	journal = {J Bacteriol},
	volume = {190},
	year = {2008},
	month = {2008 May},
	pages = {3690-9},
	abstract = {Lipoarabinomannans (LAMs) and phosphatidylinositol mannosides (PIMs) are abundant glycolipids in the cell walls of all corynebacteria and mycobacteria, including the devastating human pathogen Mycobacterium tuberculosis. We have recently shown that M. smegmatis mutants of the lipoprotein-encoding lpqW gene have a profound defect in LAM biosynthesis. When these mutants are cultured in complex medium, spontaneous bypass mutants consistently evolve in which LAM biosynthesis is restored at the expense of polar PIM synthesis. Here we show that restoration of LAM biosynthesis in the lpqW mutant results from secondary mutations in the pimE gene. PimE is a mannosyltransferase involved in converting AcPIM4, a proposed branch point intermediate in the PIM and LAM biosynthetic pathways, to more polar PIMs. Mutations in pimE arose due to insertion of the mobile genetic element ISMsm1 and independent point mutations that were clustered in predicted extracytoplasmic loops of this polytopic membrane protein. Our findings provide the first strong evidence that LpqW is required to channel intermediates such as AcPIM4 into LAM synthesis and that loss of PimE function results in the accumulation of AcPIM4, bypassing the need for LpqW. These data highlight new mechanisms regulating the biosynthetic pathways of these essential cell wall components.},
	keywords = {Cell Wall, Lipopolysaccharides, Lipoproteins, Mannosyltransferases, Mutation, Mycobacterium smegmatis, Phosphatidylinositols},
	issn = {1098-5530},
	doi = {10.1128/JB.00200-08},
	author = {Crellin, Paul K and Kovacevic, Svetozar and Martin, Kirstee L and Brammananth, Rajini and Morita, Yasu S and Billman-Jacobe, Helen and McConville, Malcolm J and Coppel, Ross L}
}
