Featured Publications
An essential periplasmic protein coordinates lipid trafficking and is required for asymmetric polar growth in mycobacteria
Gupta K, Gwin C, Rahlwes K, Biegas K, Wang C, Park J, Liu J, Swarts B, Morita Y, Rego E. An essential periplasmic protein coordinates lipid trafficking and is required for asymmetric polar growth in mycobacteria. ELife 2022, 11: e80395. PMID: 36346214, PMCID: PMC9678360, DOI: 10.7554/elife.80395.Peer-Reviewed Original ResearchConceptsPeriplasmic proteinsPolar growthNew cell wall materialOld poleQuantitative time-lapse imagingAsymmetric polar growthCell wall synthesisCell envelope compositionCell wall materialTime-lapse imagingCellular asymmetryEssential proteinsBacterial geneticsEssential transporterSingle geneWall synthesisLipid traffickingPopulation of cellsPlasma membraneTMM transportUnknown functionBroad functionsMycolic acidsTrehalose monomycolateEnvelope compositionMaturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape
Baranowski C, Welsh M, Sham L, Eskandarian H, Lim H, Kieser K, Wagner J, McKinney J, Fantner G, Ioerger T, Walker S, Bernhardt T, Rubin E, Rego E. Maturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape. ELife 2018, 7: e37516. PMID: 30324906, PMCID: PMC6231781, DOI: 10.7554/elife.37516.Peer-Reviewed Original ResearchConceptsPenicillin-binding proteinsAsymmetric polar growthRod-shaped bacteriaPolar growthPolar elongationShape maintenanceCell wallGenetic relationshipsDrug targetsUnusual crosslinksD-transpeptidasesSingle cellsPeptidoglycanCellsCrosslinksProteinMycobacteriaBacteriaPathogensTypes of crosslinksElongationGrowthMaintenanceTargetDeletion of a mycobacterial divisome factor collapses single-cell phenotypic heterogeneity
Rego E, Audette R, Rubin E. Deletion of a mycobacterial divisome factor collapses single-cell phenotypic heterogeneity. Nature 2017, 546: 153-157. PMID: 28569798, PMCID: PMC5567998, DOI: 10.1038/nature22361.Peer-Reviewed Original Research
2022
Cell Wall Damage Reveals Spatial Flexibility in Peptidoglycan Synthesis and a Nonredundant Role for RodA in Mycobacteria
Melzer E, Kado T, García-Heredia A, Gupta K, Meniche X, Morita Y, Sassetti C, Rego E, Siegrist M. Cell Wall Damage Reveals Spatial Flexibility in Peptidoglycan Synthesis and a Nonredundant Role for RodA in Mycobacteria. Journal Of Bacteriology 2022, 204: e00540-21. PMID: 35543537, PMCID: PMC9210966, DOI: 10.1128/jb.00540-21.Peer-Reviewed Original ResearchConceptsPenicillin binding proteinsCell wall damagePeptidoglycan synthesisPeptidoglycan assemblyClass A Penicillin-Binding ProteinsNascent cell wallCell wall integrityCell wall assemblyCell-wall peptidoglycanCell wall synthesisRod-shaped bacteriaMycobacterium smegmatisPolar growthInternal turgorModel organismsMreB homologsNew inhibition strategyRod complexWall synthesisWall peptidoglycanWall integrityAnimal pathogensCell wallPathway functionSubcellular distribution
2015
Phosphorylation of the Peptidoglycan Synthase PonA1 Governs the Rate of Polar Elongation in Mycobacteria
Kieser K, Boutte C, Kester J, Baer C, Barczak A, Meniche X, Chao M, Rego E, Sassetti C, Fortune S, Rubin E. Phosphorylation of the Peptidoglycan Synthase PonA1 Governs the Rate of Polar Elongation in Mycobacteria. PLOS Pathogens 2015, 11: e1005010. PMID: 26114871, PMCID: PMC4483258, DOI: 10.1371/journal.ppat.1005010.Peer-Reviewed Original ResearchConceptsPolar growthPenicillin binding proteinsCell elongationMost rod-shaped bacteriaNew cell wall materialTransglycosylase activityNormal cell lengthCell-wall peptidoglycanNew cell wallHuman pathogen Mycobacterium tuberculosisCell lengthRod-shaped bacteriaCell wall materialCell polesCell fitnessPolar elongationPathogen Mycobacterium tuberculosisWall peptidoglycanAntibiotic stressCytoplasmic regionCell wallBinding proteinPonA1Cell growthEnzymatic activity