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 ResearchMeSH KeywordsCell MembraneHumansMycobacterium tuberculosisMycolic AcidsPeriplasmPeriplasmic ProteinsConceptsPeriplasmic 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 composition
2022
Mycobacterial serine/threonine phosphatase PstP is phosphoregulated and localized to mediate control of cell wall metabolism
Shamma F, Rego E, Boutte C. Mycobacterial serine/threonine phosphatase PstP is phosphoregulated and localized to mediate control of cell wall metabolism. Molecular Microbiology 2022, 118: 47-60. PMID: 35670057, PMCID: PMC10070032, DOI: 10.1111/mmi.14951.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCell WallMycobacterium tuberculosisPeptidoglycanPhosphoprotein PhosphatasesPhosphorylationSerineConceptsCell wall metabolismWall metabolismCell wall-related proteinsSerine/threonine proteinCell wall regulationPhosphomimetic mutationReversible phosphorylationThreonine phosphataseEnvironmental stressRegulatory proteinsCell wallCorresponding mutationMycobacterial cell wallAntibiotic toleranceNovel substrateFhaAProteinPstPMycobacterium smegmatisWag31Certain substratesPeptidoglycanPhosphorylationRegulationMajor mechanism
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 ResearchMeSH KeywordsCell CycleCell DivisionCell Growth ProcessesCell WallMycobacterium smegmatisMycobacterium tuberculosisPenicillin-Binding ProteinsPeptidoglycanPhosphorylationConceptsPolar 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
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