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EstG is a novel esterase required for cell envelope integrity in Caulobacter
Department of Biological Chemistry, Johns Hopkins University School of Medicine, MD, Baltimore, United States.
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, MD, Baltimore, United States.
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, MD, Baltimore, United States.
Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet).ORCID-id: 0000-0003-2429-7542
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2023 (Engelska)Ingår i: Current Biology, ISSN 0960-9822, E-ISSN 1879-0445, Vol. 33, nr 2, s. 228-240.e7Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Proper regulation of the bacterial cell envelope is critical for cell survival. Identification and characterization of enzymes that maintain cell envelope homeostasis is crucial, as they can be targets for effective antibiotics. In this study, we have identified a novel enzyme, called EstG, whose activity protects cells from a variety of lethal assaults in the ⍺-proteobacterium Caulobacter crescentus. Despite homology to transpeptidase family cell wall enzymes and an ability to protect against cell-wall-targeting antibiotics, EstG does not demonstrate biochemical activity toward cell wall substrates. Instead, EstG is genetically connected to the periplasmic enzymes OpgH and BglX, responsible for synthesis and hydrolysis of osmoregulated periplasmic glucans (OPGs), respectively. The crystal structure of EstG revealed similarities to esterases and transesterases, and we demonstrated esterase activity of EstG in vitro. Using biochemical fractionation, we identified a cyclic hexamer of glucose as a likely substrate of EstG. This molecule is the first OPG described in Caulobacter and establishes a novel class of OPGs, the regulation and modification of which are important for stress survival and adaptation to fluctuating environments. Our data indicate that EstG, BglX, and OpgH comprise a previously unknown OPG pathway in Caulobacter. Ultimately, we propose that EstG is a novel enzyme that instead of acting on the cell wall, acts on cyclic OPGs to provide resistance to a variety of cellular stresses.

Ort, förlag, år, upplaga, sidor
Cell Press, 2023. Vol. 33, nr 2, s. 228-240.e7
Nyckelord [en]
antibiotics, Caulobacter crescentus, cell envelope, envelope stress, esterase, Gram-negative, osmoregulated periplasmic glucans, peptidoglycan, transesterase
Nationell ämneskategori
Mikrobiologi
Identifikatorer
URN: urn:nbn:se:umu:diva-212079DOI: 10.1016/j.cub.2022.11.037PubMedID: 36516849Scopus ID: 2-s2.0-85146361157OAI: oai:DiVA.org:umu-212079DiVA, id: diva2:1782825
Forskningsfinansiär
NIH (National Institutes of Health)VetenskapsrådetKnut och Alice Wallenbergs StiftelseKempestiftelsernaTillgänglig från: 2023-07-17 Skapad: 2023-07-17 Senast uppdaterad: 2023-07-17Bibliografiskt granskad

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Alvarez, Laura

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Alvarez, LauraCava, Felipe
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Molekylär Infektionsmedicin, Sverige (MIMS)Umeå Centre for Microbial Research (UCMR)Institutionen för molekylärbiologi (Medicinska fakulteten)Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet)
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